Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T02702 Target Info
Target Name Bacterial Dihydrofolate reductase (Bact DHFR)
Synonyms Bact Dihydrofolate reductase
Target Type Clinical trial Target
Gene Name Bact DHFR
UniProt ID
DYR_ECOLI
Ligand General Information  Top
Ligand Name NADP+ Ligand Info
Canonical SMILES C1=CC(=C[N+](=C1)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OCC3C(C(C(O3)N4C=NC5=C(N=CN=C54)N)OP(=O)(O)O)O)O)O)C(=O)N
InChI 1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/p+1/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKey XJLXINKUBYWONI-NNYOXOHSSA-O
PubChem Compound ID 5886
Drug Binding Sites of Target  Top
PDB ID: 4KJJ      Cryogenic WT DHFR
Method X-ray diffraction Resolution 1.15 Å Mutation No [1]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Residue
Distance (Å)
ILE5
4.438
ALA6
2.548
ALA7
1.830
LEU8
4.185
ILE14
2.027
GLY15
2.406
MET16
3.411
GLU17
4.111
ASN18
1.834
ALA19
2.847
MET20
2.389
TRP22
2.200
MET42
4.925
GLY43
2.574
ARG44
1.647
HIS45
1.856
THR46
1.771
TRP47
4.756
SER49
2.474
ILE50
4.851
Residue
Distance (Å)
LEU62
2.361
SER63
1.685
SER64
1.734
GLN65
1.943
VAL75
4.415
LYS76
2.798
SER77
2.746
VAL78
2.732
ILE94
2.233
GLY95
2.401
GLY96
2.069
GLY97
2.578
ARG98
1.802
VAL99
2.327
TYR100
2.649
GLN102
1.920
ILE115
4.973
ASP122
4.275
THR123
2.303
PDB ID: 4NX7      single cryogenic temperature model of DHFR
Method X-ray diffraction Resolution 1.15 Å Mutation No [2]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Residue
Distance (Å)
ILE5
4.404
ALA6
2.686
ALA7
1.997
LEU8
4.249
ILE14
2.064
GLY15
2.503
MET16
3.464
GLU17
4.227
ASN18
2.116
ALA19
3.114
MET20
2.572
TRP22
2.361
GLY43
2.673
ARG44
1.972
HIS45
2.263
THR46
1.947
TRP47
4.832
SER49
2.331
LEU62
2.315
Residue
Distance (Å)
SER63
1.805
SER64
1.896
GLN65
3.550
VAL75
4.449
LYS76
2.758
SER77
2.835
VAL78
2.671
ILE94
2.246
GLY95
2.392
GLY96
2.202
GLY97
2.696
ARG98
2.148
VAL99
2.427
TYR100
2.554
GLN102
1.880
ILE115
4.956
ASP122
4.062
THR123
2.441
PDB ID: 5CC9      L28F E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate
Method X-ray diffraction Resolution 1.20 Å Mutation Yes [3]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADFAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Residue
Distance (Å)
GLY15
4.667
MET16
2.197
GLY43
2.680
ARG44
1.788
HIS45
2.140
THR46
1.973
TRP47
4.667
LEU62
2.179
SER63
1.734
SER64
1.892
GLN65
3.739
VAL75
4.497
Residue
Distance (Å)
LYS76
2.871
SER77
2.821
VAL78
2.640
GLY95
4.020
GLY96
2.268
GLY97
2.278
ARG98
2.159
VAL99
2.644
GLN102
1.910
ASP122
3.076
THR123
2.326
PDB ID: 4KJK      Room Temperature WT DHFR
Method X-ray diffraction Resolution 1.35 Å Mutation No [1]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:8 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:115 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.323
ALA6
2.576
ALA7
1.881
LEU8
4.133
VAL13
4.959
ILE14
1.856
GLY15
2.402
MET16
3.465
GLU17
4.205
ASN18
1.943
ALA19
3.048
MET20
2.939
TRP22
2.317
GLY43
2.526
ARG44
1.582
HIS45
2.267
THR46
1.705
TRP47
4.869
SER49
2.823
Residue
Distance (Å)
LEU62
2.289
SER63
2.305
SER64
1.973
GLN65
3.998
VAL75
4.460
LYS76
2.869
SER77
2.927
VAL78
2.566
ILE94
2.226
GLY95
2.513
GLY96
1.850
GLY97
2.447
ARG98
1.721
VAL99
2.321
TYR100
2.563
GLN102
1.929
ILE115
4.959
ASP122
4.248
THR123
2.079
PDB ID: 4NX6      single room temperature model of DHFR
Method X-ray diffraction Resolution 1.35 Å Mutation No [2]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:8 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.403
ALA6
2.720
ALA7
2.075
LEU8
4.330
ILE14
2.142
GLY15
2.645
MET16
3.481
GLU17
4.074
ASN18
1.906
ALA19
2.676
MET20
2.952
TRP22
2.434
GLY43
2.561
ARG44
2.014
HIS45
2.253
THR46
1.847
TRP47
4.914
SER49
2.678
Residue
Distance (Å)
LEU62
2.344
SER63
1.890
SER64
1.928
GLN65
3.497
VAL75
4.493
LYS76
2.422
SER77
2.944
VAL78
2.658
ILE94
2.236
GLY95
2.467
GLY96
2.055
GLY97
2.632
ARG98
2.269
VAL99
2.536
TYR100
2.647
GLN102
1.761
ASP122
4.744
THR123
2.527
PDB ID: 5CCC      wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate
Method X-ray diffraction Resolution 1.50 Å Mutation No [3]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:14 or .A:15 or .A:16 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:61 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE14
4.926
GLY15
4.838
MET16
2.080
GLY43
2.724
ARG44
1.734
HIS45
1.909
THR46
1.872
TRP47
4.712
ILE61
4.964
LEU62
2.236
SER63
1.828
SER64
1.894
GLN65
3.523
Residue
Distance (Å)
VAL75
4.479
LYS76
3.044
SER77
2.981
VAL78
3.094
GLY95
3.915
GLY96
2.257
GLY97
2.216
ARG98
2.139
VAL99
2.578
GLN102
1.918
ASP122
2.025
THR123
2.579
PDB ID: 1RA9      DIHYDROFOLATE REDUCTASE COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 1.55 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY43
3.470
ARG44
2.621
HIS45
3.330
THR46
2.748
LEU62
3.213
SER63
2.524
SER64
2.695
GLN65
4.339
VAL75
4.909
LYS76
3.419
Residue
Distance (Å)
SER77
4.097
VAL78
4.085
GLY95
4.134
GLY96
3.139
GLY97
2.954
ARG98
2.871
VAL99
3.497
GLN102
2.787
THR123
3.740
PDB ID: 1RA2      DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 1.60 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.901
ALA6
3.399
ALA7
2.795
ILE14
3.102
GLY15
3.585
MET16
3.569
TRP22
4.818
GLY43
3.445
ARG44
2.810
HIS45
3.091
THR46
2.764
SER49
3.958
LEU62
3.291
SER63
2.531
SER64
2.741
Residue
Distance (Å)
GLN65
4.493
VAL75
4.925
LYS76
3.372
SER77
4.032
VAL78
3.887
ILE94
3.084
GLY95
3.617
GLY96
3.018
GLY97
3.113
ARG98
2.935
VAL99
3.441
TYR100
2.903
GLN102
2.717
THR123
3.881
PDB ID: 7D4L      X-ray crystal Structure of E.coli Dihydrofolate Reductase complexed with folate and NADP+ at pH7.0
Method X-ray diffraction Resolution 1.60 Å Mutation No [5]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.736
ALA6
3.400
ALA7
2.759
ILE14
3.007
GLY15
3.611
MET16
3.935
GLU17
4.904
ASN18
3.310
ALA19
3.463
MET20
3.538
TRP22
3.719
GLY43
3.475
ARG44
2.493
HIS45
3.261
THR46
2.732
SER49
3.652
LEU62
3.266
Residue
Distance (Å)
SER63
2.723
SER64
2.726
GLN65
3.532
VAL75
4.957
LYS76
3.389
SER77
4.005
VAL78
3.893
ILE94
3.066
GLY95
3.865
GLY96
2.936
GLY97
3.089
ARG98
2.941
VAL99
3.282
TYR100
3.177
GLN102
2.807
ASP122
4.806
THR123
3.886
PDB ID: 7D4X      X-ray crystal Structure of E.coli Dihydrofolate Reductase complexed with folate and NADP+ at pH7.0
Method X-ray diffraction Resolution 1.60 Å Mutation No [5]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.787
ALA6
3.489
ALA7
2.880
ILE14
2.996
GLY15
3.649
MET16
3.763
GLU17
4.929
ASN18
3.372
ALA19
3.654
TRP22
3.804
GLY43
3.453
ARG44
2.353
HIS45
3.422
THR46
2.688
SER49
4.109
LEU62
3.283
SER63
2.894
Residue
Distance (Å)
SER64
2.731
GLN65
4.630
VAL75
4.929
LYS76
3.420
SER77
3.988
VAL78
4.285
ILE94
3.130
GLY95
3.840
GLY96
2.907
GLY97
3.082
ARG98
2.916
VAL99
3.277
TYR100
3.211
GLN102
3.030
ASP122
4.807
THR123
3.967
PDB ID: 7D3Z      X-ray crystal Structure of E.coli Dihydrofolate Reductase complexed with folate and NADP+ at pH4.5
Method X-ray diffraction Resolution 1.65 Å Mutation No [5]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.749
ALA6
3.317
ALA7
2.775
ILE14
2.992
GLY15
3.475
MET16
3.867
GLU17
4.950
ASN18
3.383
ALA19
3.477
MET20
3.058
TRP22
3.702
GLY43
3.510
ARG44
2.616
HIS45
3.131
THR46
2.682
SER49
3.544
LEU62
3.212
Residue
Distance (Å)
SER63
2.611
SER64
2.678
GLN65
4.082
VAL75
4.989
LYS76
3.207
SER77
4.078
VAL78
4.003
ILE94
3.083
GLY95
3.870
GLY96
2.914
GLY97
2.991
ARG98
2.977
VAL99
3.242
TYR100
3.155
GLN102
2.785
ASP122
4.837
THR123
3.926
PDB ID: 7D49      X-ray crystal Structure of E.coli Dihydrofolate Reductase complexed with folate and NADP+ at pH4.5
Method X-ray diffraction Resolution 1.65 Å Mutation No [5]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:8 or .A:14 or .A:15 or .A:16 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.751
ALA6
3.473
ALA7
2.623
LEU8
4.869
ILE14
2.972
GLY15
3.502
MET16
3.830
ASN18
3.105
ALA19
3.408
MET20
3.762
TRP22
3.962
GLY43
3.398
ARG44
2.411
HIS45
2.912
THR46
2.724
SER49
3.817
LEU62
3.236
Residue
Distance (Å)
SER63
2.827
SER64
2.502
GLN65
4.588
VAL75
4.838
LYS76
3.292
SER77
3.950
VAL78
3.752
ILE94
3.115
GLY95
3.803
GLY96
2.832
GLY97
3.054
ARG98
2.972
VAL99
3.312
TYR100
3.242
GLN102
2.917
ASP122
4.935
THR123
3.714
PDB ID: 7D6G      Neutron crystal Structure of E.coli Dihydrofolate Reductase complexed with folate and NADP+ at pH4.5
Method X-ray diffraction Resolution 1.65 Å Mutation No [5]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:8 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.251
ALA6
2.588
ALA7
1.936
LEU8
4.182
ILE14
2.100
GLY15
2.593
MET16
3.251
GLU17
4.550
ASN18
2.296
ALA19
2.711
MET20
3.231
TRP22
2.504
GLY43
2.681
ARG44
1.882
HIS45
2.200
THR46
1.834
TRP47
4.839
SER49
2.617
Residue
Distance (Å)
LEU62
2.343
SER63
2.317
SER64
2.087
GLN65
3.414
VAL75
4.668
LYS76
2.827
SER77
2.871
VAL78
2.843
ILE94
2.159
GLY95
2.299
GLY96
2.055
GLY97
2.545
ARG98
2.181
VAL99
2.476
TYR100
2.429
GLN102
1.936
ASP122
4.882
THR123
2.860
PDB ID: 7LVC      E. coli DHFR by Native Mn,P,S-SAD at Room Temperature
Method X-ray diffraction Resolution 1.70 Å Mutation No [6]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:8 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.339
ALA6
2.617
ALA7
2.041
LEU8
4.310
ILE14
2.115
GLY15
2.534
MET16
3.469
GLU17
4.423
ASN18
2.131
ALA19
2.765
MET20
2.975
TRP22
2.616
GLY43
2.663
ARG44
1.737
HIS45
2.372
THR46
2.248
TRP47
4.785
SER49
2.106
Residue
Distance (Å)
LEU62
2.335
SER63
2.385
SER64
1.935
GLN65
3.482
VAL75
4.648
LYS76
2.947
SER77
3.056
VAL78
2.790
ILE94
2.242
GLY95
2.413
GLY96
2.211
GLY97
2.605
ARG98
2.226
VAL99
2.501
TYR100
2.570
GLN102
1.959
ASP122
4.091
THR123
2.218
PDB ID: 1RA3      DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 1.80 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY43
3.506
ARG44
2.592
HIS45
3.340
THR46
2.758
LEU62
3.216
SER63
2.535
SER64
2.788
GLN65
4.448
VAL75
4.945
LYS76
3.482
Residue
Distance (Å)
SER77
4.202
VAL78
4.136
GLY95
4.193
GLY96
3.111
GLY97
2.834
ARG98
2.971
VAL99
3.350
GLN102
2.857
ASP122
4.870
THR123
3.636
PDB ID: 1RX2      DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH WITH FOLATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 1.80 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.630
ALA6
3.278
ALA7
2.798
ILE14
3.094
GLY15
3.472
MET16
3.644
GLU17
4.648
ASN18
3.195
ALA19
3.248
MET20
3.328
TRP22
3.818
GLY43
3.547
ARG44
2.676
HIS45
2.914
THR46
2.573
SER49
3.819
LEU62
2.960
Residue
Distance (Å)
SER63
2.312
SER64
2.771
GLN65
4.085
VAL75
4.997
LYS76
3.136
SER77
3.869
VAL78
3.916
ILE94
2.807
GLY95
3.675
GLY96
2.983
GLY97
3.184
ARG98
3.186
VAL99
3.343
TYR100
2.980
GLN102
2.525
ASP122
4.643
THR123
3.805
PDB ID: 3QL3      Re-refined coordinates for PDB entry 1RX2
Method X-ray diffraction Resolution 1.80 Å Mutation No [7]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.591
ALA6
3.292
ALA7
2.738
ILE14
2.944
GLY15
3.475
MET16
3.645
GLU17
4.900
ASN18
3.437
ALA19
3.550
MET20
3.464
TRP22
3.722
GLY43
3.431
ARG44
2.923
HIS45
3.238
THR46
2.685
SER49
3.950
LEU62
3.131
Residue
Distance (Å)
SER63
2.572
SER64
2.624
GLN65
4.098
VAL75
4.854
LYS76
3.139
SER77
3.903
VAL78
3.920
ILE94
2.927
GLY95
3.772
GLY96
2.789
GLY97
3.052
ARG98
2.986
VAL99
3.324
TYR100
3.236
GLN102
2.692
ASP122
4.717
THR123
3.923
PDB ID: 1RA1      DIHYDROFOLATE REDUCTASE COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (REDUCED FORM)
Method X-ray diffraction Resolution 1.90 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY43
3.506
ARG44
2.696
HIS45
3.211
THR46
2.626
LEU62
3.216
SER63
2.502
SER64
2.686
GLN65
4.354
VAL75
4.983
LYS76
3.488
Residue
Distance (Å)
SER77
4.039
VAL78
3.993
GLY95
3.995
GLY96
3.115
GLY97
3.187
ARG98
2.911
VAL99
3.534
GLN102
2.733
THR123
3.724
PDB ID: 1RC4      DIHYDROFOLATE REDUCTASE COMPLEXED WITH 5,10-DIDEAZATETRAHYDROFOLATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 1.90 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:16 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET16
3.083
GLY43
3.422
ARG44
2.704
HIS45
3.250
THR46
2.536
LEU62
3.039
SER63
2.508
SER64
2.433
GLN65
4.099
LYS76
3.558
Residue
Distance (Å)
SER77
4.308
VAL78
4.137
GLY95
3.893
GLY96
2.799
GLY97
2.654
ARG98
3.277
VAL99
3.317
GLN102
2.867
ASP122
2.917
THR123
3.335
PDB ID: 1RX9      DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 1.90 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:8 or .A:14 or .A:15 or .A:17 or .A:18 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.600
ALA6
3.239
ALA7
2.704
LEU8
4.890
ILE14
2.856
GLY15
4.659
GLU17
3.977
ASN18
3.268
MET20
3.776
TRP22
4.056
GLY43
3.400
ARG44
2.742
HIS45
3.037
THR46
2.644
LEU62
2.789
SER63
2.571
Residue
Distance (Å)
SER64
2.381
GLN65
2.608
VAL75
4.820
LYS76
3.247
SER77
4.256
VAL78
4.293
ILE94
2.861
GLY95
3.393
GLY96
2.875
GLY97
3.499
ARG98
3.001
VAL99
3.447
TYR100
2.785
GLN102
2.833
ASP122
2.952
THR123
4.054
PDB ID: 1RX1      DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (REDUCED FORM)
Method X-ray diffraction Resolution 2.00 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.599
ALA6
3.291
ALA7
2.685
ILE14
3.051
GLY15
3.588
MET16
3.537
GLU17
4.285
ASN18
3.021
ALA19
3.141
MET20
3.649
TRP22
4.056
GLY43
3.536
ARG44
2.675
HIS45
3.123
THR46
2.591
LEU62
2.768
SER63
2.800
Residue
Distance (Å)
SER64
2.508
GLN65
4.429
VAL75
4.628
LYS76
3.341
SER77
4.072
VAL78
4.455
ILE94
2.773
GLY95
3.249
GLY96
2.977
GLY97
3.273
ARG98
2.920
VAL99
3.334
TYR100
2.862
GLN102
3.099
ASP122
4.613
THR123
4.161
PDB ID: 1RX6      DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH 5,10-DIDEAZATETRAHYDROFOLATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (REDUCED FORM)
Method X-ray diffraction Resolution 2.00 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:16 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET16
4.185
GLY43
3.587
ARG44
2.726
HIS45
2.972
THR46
2.638
LEU62
2.769
SER63
2.261
SER64
2.728
GLN65
2.876
VAL75
4.617
LYS76
2.823
Residue
Distance (Å)
SER77
4.185
VAL78
4.532
GLY95
4.001
GLY96
2.859
GLY97
2.959
ARG98
3.759
VAL99
3.838
GLN102
2.971
ASP122
3.850
THR123
4.666
PDB ID: 1RB2      DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 2.10 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.790
ALA6
3.187
ALA7
2.406
ILE14
2.953
GLY15
3.655
MET16
3.259
TRP22
4.928
GLY43
3.589
ARG44
2.583
HIS45
3.061
THR46
2.809
SER49
4.543
LEU62
3.353
SER63
3.196
Residue
Distance (Å)
SER64
2.488
GLN65
4.279
LYS76
3.182
SER77
4.109
VAL78
4.186
ILE94
3.110
GLY95
3.133
GLY96
3.000
GLY97
3.115
ARG98
3.208
VAL99
3.297
TYR100
2.770
GLN102
2.524
THR123
3.776
PDB ID: 1RX3      DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (REDUCED FORM)
Method X-ray diffraction Resolution 2.20 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:42 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.630
ALA6
3.636
ALA7
2.975
ILE14
3.232
GLY15
3.510
MET16
3.697
GLU17
4.640
ASN18
3.311
ALA19
3.262
MET20
3.651
TRP22
3.940
MET42
4.987
GLY43
3.445
ARG44
2.467
HIS45
2.945
THR46
2.491
SER49
4.279
LEU62
2.842
Residue
Distance (Å)
SER63
2.291
SER64
2.722
GLN65
3.581
VAL75
4.898
LYS76
3.150
SER77
4.017
VAL78
3.957
ILE94
3.031
GLY95
3.710
GLY96
2.920
GLY97
3.031
ARG98
3.181
VAL99
3.482
TYR100
3.449
GLN102
2.747
ASP122
4.655
THR123
3.918
PDB ID: 1RX4      DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH 5,10-DIDEAZATETRAHYDROFOLATE AND 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
Method X-ray diffraction Resolution 2.20 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY43
3.386
ARG44
2.796
HIS45
2.975
THR46
2.768
LEU62
2.958
SER63
2.648
SER64
2.548
GLN65
2.272
VAL75
4.571
LYS76
2.983
Residue
Distance (Å)
SER77
4.004
VAL78
4.350
GLY95
4.009
GLY96
2.869
GLY97
2.973
ARG98
3.623
VAL99
3.768
GLN102
2.883
ASP122
2.294
THR123
3.777
PDB ID: 1DRH      ISOMORPHOUS CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE, 5-DEAZAFOLATE AND 5,10-DIDEAZATETRAHYDROFOLATE: MECHANISTIC IMPLICATIONS
Method X-ray diffraction Resolution 2.30 Å Mutation No [8]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.251
ALA6
3.084
ALA7
2.644
ILE14
3.094
GLY15
3.551
MET16
3.764
GLU17
4.878
ASN18
3.218
ALA19
3.025
MET20
3.694
TRP22
3.984
GLY43
3.608
ARG44
2.288
HIS45
2.756
THR46
2.475
SER49
4.574
LEU62
3.217
Residue
Distance (Å)
SER63
2.277
SER64
2.923
GLN65
3.926
VAL75
4.685
LYS76
3.198
SER77
4.274
VAL78
3.625
ILE94
2.943
GLY95
3.652
GLY96
3.008
GLY97
2.886
ARG98
2.728
VAL99
2.994
TYR100
3.088
GLN102
3.141
ASP122
4.674
THR123
4.049
PDB ID: 1RB3      DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 2.30 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:16 or .A:17 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET16
3.651
GLU17
4.461
GLY43
3.517
ARG44
2.921
HIS45
2.969
THR46
2.820
LEU62
3.425
SER63
2.552
SER64
2.669
GLN65
4.537
LYS76
3.224
Residue
Distance (Å)
SER77
4.196
VAL78
3.929
GLY95
4.046
GLY96
2.921
GLY97
2.682
ARG98
3.013
VAL99
3.284
GLN102
2.659
ASP122
2.773
THR123
3.524
PDB ID: 1RH3      DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (REDUCED FORM)
Method X-ray diffraction Resolution 2.40 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.374
ALA6
3.304
ALA7
2.792
ILE14
3.093
GLY15
3.876
MET16
3.941
GLU17
4.749
ASN18
3.293
ALA19
2.587
MET20
3.002
TRP22
3.797
GLY43
3.741
ARG44
2.903
HIS45
2.421
THR46
2.401
SER49
4.225
LEU62
3.242
Residue
Distance (Å)
SER63
2.278
SER64
2.828
GLN65
3.718
VAL75
4.643
LYS76
3.325
SER77
4.194
VAL78
4.053
ILE94
2.793
GLY95
3.496
GLY96
2.801
GLY97
2.706
ARG98
2.864
VAL99
2.794
TYR100
3.072
GLN102
3.638
THR123
4.045
PDB ID: 6DFR      CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE
Method X-ray diffraction Resolution 2.40 Å Mutation No [9]
PDB Sequence
MISLIAALAV
10
DRVIGPWNLP
25
ADLAWFKRNT
35
LDKPVIMGRH
45
TWESIGRPLP
55

GRKNIILSSQ
65
PGTDDRVTWV
75
KSVDEAIAAC
85
GDVPEIMVIG
95
GGRVYEQFLP
105

KAQKLYLTHI
115
DAEVEGDTHF
125
PDYEPDDWES
135
VFSEFHDADA
145
QNSHSYCFEI
155

LERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:14 or .A:15 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE14
3.693
GLY15
3.941
GLY43
3.524
ARG44
2.561
HIS45
3.370
THR46
2.529
LEU62
2.797
SER63
2.797
SER64
2.756
GLN65
4.359
LYS76
3.565
Residue
Distance (Å)
SER77
4.186
VAL78
3.855
GLY95
3.778
GLY96
2.810
GLY97
2.946
ARG98
3.136
VAL99
3.024
GLN102
2.671
ASP122
4.238
THR123
3.496
PDB ID: 7DFR      CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE
Method X-ray diffraction Resolution 2.50 Å Mutation No [9]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.361
ALA6
3.196
ALA7
2.936
ILE14
3.333
GLY15
3.809
MET16
3.482
GLU17
3.825
ASN18
3.209
ALA19
3.167
MET20
3.629
TRP22
3.613
GLY43
3.659
ARG44
2.643
HIS45
2.109
THR46
2.269
SER49
3.688
LEU62
2.980
Residue
Distance (Å)
SER63
2.307
SER64
3.034
GLN65
4.086
VAL75
4.707
LYS76
3.149
SER77
4.217
VAL78
3.826
ILE94
2.972
GLY95
3.775
GLY96
2.843
GLY97
2.559
ARG98
2.862
VAL99
3.056
TYR100
2.919
GLN102
3.374
THR123
3.718
PDB ID: 1DRE      DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE AND NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED FORM)
Method X-ray diffraction Resolution 2.60 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.450
ALA6
3.322
ALA7
2.683
ILE14
3.079
GLY15
3.916
MET16
3.989
GLU17
3.426
ASN18
3.301
ALA19
2.610
MET20
3.293
TRP22
3.904
GLY43
3.615
ARG44
2.967
HIS45
2.357
THR46
2.445
SER49
4.202
LEU62
3.164
Residue
Distance (Å)
SER63
2.414
SER64
2.904
GLN65
3.745
VAL75
4.775
LYS76
3.309
SER77
4.162
VAL78
4.139
ILE94
2.740
GLY95
3.587
GLY96
2.857
GLY97
2.754
ARG98
2.942
VAL99
2.893
TYR100
2.847
GLN102
3.635
THR123
3.827
PDB ID: 1RX8      DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
Method X-ray diffraction Resolution 2.80 Å Mutation No [4]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLDKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:18 or .A:42 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASN18
4.283
MET42
4.905
GLY43
3.258
ARG44
3.165
HIS45
2.821
THR46
2.311
TRP47
4.467
LEU62
2.777
SER63
2.393
SER64
2.460
GLN65
3.684
Residue
Distance (Å)
LYS76
3.083
SER77
3.970
VAL78
4.215
GLY95
3.617
GLY96
2.550
GLY97
3.327
ARG98
3.492
VAL99
3.364
GLN102
2.300
THR123
4.879
PDB ID: 4FHB      Enhancing DHFR catalysis by binding of an allosteric regulator nanobody (Nb179)
Method X-ray diffraction Resolution 2.80 Å Mutation No [10]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:8 or .A:14 or .A:15 or .A:16 or .A:18 or .A:20 or .A:22 or .A:42 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.845
ALA6
3.366
ALA7
2.632
LEU8
4.951
ILE14
2.851
GLY15
3.969
MET16
3.524
ASN18
4.939
MET20
4.981
TRP22
4.645
MET42
4.961
GLY43
3.247
ARG44
2.695
HIS45
2.547
THR46
3.034
SER49
3.644
Residue
Distance (Å)
LEU62
3.125
SER63
2.291
SER64
2.679
GLN65
3.241
LYS76
3.263
SER77
4.069
VAL78
3.476
ILE94
3.076
GLY95
3.440
GLY96
2.513
GLY97
2.976
ARG98
2.901
VAL99
3.842
TYR100
3.224
GLN102
3.100
THR123
3.437
PDB ID: 7MYM      Crystal structure of Escherichia coli dihydrofolate reductase in complex with TRIMETHOPRIM and NADPH
Method X-ray diffraction Resolution 3.04 Å Mutation No [11]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILER
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:27 or .A:42 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ALA6
4.082
ALA7
3.046
ILE14
3.073
GLY15
3.398
MET16
3.804
GLU17
4.930
ASN18
3.392
ALA19
2.989
MET20
3.296
TRP22
4.246
ASP27
4.989
MET42
4.898
GLY43
3.121
ARG44
2.808
HIS45
3.043
THR46
2.831
TRP47
4.892
SER49
3.631
Residue
Distance (Å)
LEU62
2.907
SER63
2.064
SER64
2.564
GLN65
4.320
LYS76
2.802
SER77
4.374
VAL78
4.056
ILE94
3.205
GLY95
3.725
GLY96
2.984
GLY97
3.063
ARG98
2.557
VAL99
3.450
TYR100
3.589
GLN102
3.274
ASP122
4.255
THR123
3.275
PDB ID: 4KJL      Room Temperature N23PPS148A DHFR
Method X-ray diffraction Resolution 1.38 Å Mutation Yes [1]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWPPLPADLA
30
WFKRNTLNKP
40
VIMGRHTWES
50

IGRPLPGRKN
60
IILSSQPGTD
70
DRVTWVKSVD
80
EAIAACGDVP
90
EIMVIGGGRV
100

YEQFLPKAQK
110
LYLTHIDAEV
120
EGDTHFPDYE
130
PDDWESVFSE
140
FHDADAQNAH
150

SYCFEILERR
160
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:8 or .A:13 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:21 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:48 or .A:50 or .A:62 or .A:63 or .A:64 or .A:65 or .A:66 or .A:76 or .A:77 or .A:78 or .A:79 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:101 or .A:103 or .A:123 or .A:124; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.376
ALA6
2.672
ALA7
1.816
LEU8
4.050
VAL13
4.884
ILE14
2.008
GLY15
2.540
MET16
3.211
GLU17
4.111
ASN18
1.732
ALA19
2.869
MET20
2.384
PRO21
4.613
TRP22
2.280
MET43
4.981
GLY44
2.555
ARG45
1.575
HIS46
2.325
THR47
1.712
TRP48
4.935
Residue
Distance (Å)
SER50
3.107
ILE62
4.997
LEU63
2.274
SER64
1.739
SER65
1.878
GLN66
3.185
VAL76
4.394
LYS77
2.766
SER78
2.885
VAL79
2.198
ILE95
2.169
GLY96
2.367
GLY97
1.668
GLY98
2.342
ARG99
1.735
VAL100
2.283
TYR101
2.574
GLN103
1.872
ASP123
4.485
THR124
2.278
PDB ID: 4X5F      ecDHFR complexed with folate and NADP+ at 0.1 MPa
Method X-ray diffraction Resolution 1.70 Å Mutation No [12]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.746
ALA6
3.366
ALA7
2.869
ILE14
3.007
GLY15
3.558
MET16
3.830
GLY43
3.502
ARG44
2.840
HIS45
3.035
THR46
2.652
SER49
3.846
LEU62
3.240
SER63
2.611
SER64
2.739
GLN65
4.485
Residue
Distance (Å)
VAL75
4.953
LYS76
3.369
SER77
4.076
VAL78
4.037
ILE94
3.128
GLY95
3.774
GLY96
2.990
GLY97
3.256
ARG98
2.907
VAL99
3.392
TYR100
3.223
GLN102
2.818
ASP122
4.940
THR123
3.846
PDB ID: 4X5I      ecDHFR complexed with folate and NADP+ at 660 MPa
Method X-ray diffraction Resolution 1.80 Å Mutation No [12]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:16 or .A:17 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET16
4.198
GLU17
4.673
GLY43
3.474
ARG44
3.010
HIS45
3.212
THR46
2.896
LEU62
3.244
SER63
2.302
SER64
2.757
GLN65
4.309
VAL75
4.826
Residue
Distance (Å)
LYS76
3.394
SER77
3.919
VAL78
3.840
GLY95
3.873
GLY96
2.892
GLY97
3.178
ARG98
3.046
VAL99
3.390
GLN102
2.744
ASP122
2.813
THR123
3.584
PDB ID: 5Z6F      High-pressure Crystal Structure Analysis of DHFR(0.1 MPa)
Method X-ray diffraction Resolution 1.80 Å Mutation No [12]
PDB Sequence
HMISLIAALA
9
VDRVIGMENA
19
MPWNLPADLA
29
WFKRNTLNKP
39
VIMGRHTWES
49

IGRPLPGRKN
59
IILSSQPGTD
69
DRVTWVKSVD
79
EAIAACGDVP
89
EIMVIGGGRV
99

YEQFLPKAQK
109
LYLTHIDAEV
119
EGDTHFPDYE
129
PDDWESVFSE
139
FHDADAQNSH
149

SYFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.703
ALA6
3.323
ALA7
2.810
ILE14
3.024
GLY15
3.488
MET16
3.868
GLU17
4.948
ASN18
3.303
ALA19
3.370
MET20
3.560
TRP22
3.753
GLY43
3.330
ARG44
3.037
HIS45
3.032
THR46
2.618
SER49
4.000
LEU62
3.210
Residue
Distance (Å)
SER63
2.531
SER64
2.457
GLN65
4.160
VAL75
4.937
LYS76
3.228
SER77
4.111
VAL78
3.944
ILE94
3.125
GLY95
3.891
GLY96
2.935
GLY97
2.987
ARG98
2.934
VAL99
3.247
TYR100
3.095
GLN102
2.829
ASP122
4.955
THR123
3.807
PDB ID: 5Z6J      High-pressure Crystal Structure Analysis of M20 loop closed DHFR at 220 MPa
Method X-ray diffraction Resolution 1.80 Å Mutation No [12]
PDB Sequence
HMISLIAALA
9
VDRVIGMENA
19
MPWNLPADLA
29
WFKRNTLNKP
39
VIMGRHTWES
49

IGRPLPGRKN
59
IILSSQPGTD
69
DRVTWVKSVD
79
EAIAACGDVP
89
EIMVIGGGRV
99

YEQFLPKAQK
109
LYLTHIDAEV
119
EGDTHFPDYE
129
PDDWESVFSE
139
FHDADAQNSH
149

SYFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.630
ALA6
3.253
ALA7
2.792
ILE14
3.044
GLY15
3.478
MET16
3.743
GLU17
4.840
ASN18
3.199
ALA19
3.264
MET20
3.434
TRP22
3.603
GLY43
3.296
ARG44
2.500
HIS45
2.997
THR46
2.617
SER49
3.819
LEU62
3.170
Residue
Distance (Å)
SER63
2.535
SER64
2.700
GLN65
2.944
VAL75
4.934
LYS76
3.187
SER77
3.985
VAL78
3.966
ILE94
3.085
GLY95
3.810
GLY96
2.920
GLY97
2.983
ARG98
2.991
VAL99
3.301
TYR100
3.059
GLN102
2.692
ASP122
4.755
THR123
3.627
PDB ID: 5Z6K      High-pressure Crystal Structure Analysis of M20 loop closed DHFR at 400 MPa
Method X-ray diffraction Resolution 1.80 Å Mutation No [12]
PDB Sequence
HMISLIAALA
9
VDRVIGMENA
19
MPWNLPADLA
29
WFKRNTLNKP
39
VIMGRHTWES
49

IGRPLPGRKN
59
IILSSQPGTD
69
DRVTWVKSVD
79
EAIAACGDVP
89
EIMVIGGGRV
99

YEQFLPKAQK
109
LYLTHIDAEV
119
EGDTHFPDYE
129
PDDWESVFSE
139
FHDADAQNSH
149

SYFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.618
ALA6
3.231
ALA7
2.755
ILE14
3.004
GLY15
3.495
MET16
3.681
GLU17
4.785
ASN18
3.119
ALA19
3.315
MET20
3.287
TRP22
3.629
GLY43
3.247
ARG44
2.521
HIS45
2.990
THR46
2.596
SER49
3.695
LEU62
3.164
Residue
Distance (Å)
SER63
2.604
SER64
2.666
GLN65
4.392
VAL75
4.940
LYS76
3.059
SER77
4.043
VAL78
3.924
ILE94
3.028
GLY95
3.734
GLY96
2.907
GLY97
2.963
ARG98
2.935
VAL99
3.339
TYR100
2.982
GLN102
2.713
ASP122
4.778
THR123
3.642
PDB ID: 4X5J      ecDHFR complexed with folate and NADP+ at 750 MPa
Method X-ray diffraction Resolution 1.85 Å Mutation No [12]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:16 or .A:17 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET16
3.964
GLU17
4.658
GLY43
3.366
ARG44
3.010
HIS45
3.342
THR46
3.035
LEU62
3.194
SER63
2.449
SER64
2.600
GLN65
4.217
VAL75
4.894
Residue
Distance (Å)
LYS76
3.195
SER77
3.823
VAL78
3.923
GLY95
3.794
GLY96
2.823
GLY97
3.167
ARG98
2.935
VAL99
3.438
GLN102
2.534
ASP122
2.945
THR123
3.602
PDB ID: 4X5G      ecDHFR complexed with folate and NADP+ at 270 MPa
Method X-ray diffraction Resolution 1.90 Å Mutation No [12]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.768
ALA6
3.368
ALA7
2.822
ILE14
2.935
GLY15
3.426
MET16
3.612
GLY43
3.504
ARG44
2.828
HIS45
3.099
THR46
2.727
SER49
3.533
LEU62
3.235
SER63
2.651
SER64
2.688
GLN65
4.346
Residue
Distance (Å)
VAL75
4.828
LYS76
3.315
SER77
4.080
VAL78
3.987
ILE94
3.083
GLY95
3.733
GLY96
2.964
GLY97
3.077
ARG98
2.866
VAL99
3.410
TYR100
3.219
GLN102
2.686
ASP122
4.901
THR123
3.826
PDB ID: 4X5H      ecDHFR complexed with folate and NADP+ at 500 MPa
Method X-ray diffraction Resolution 1.90 Å Mutation No [12]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:16 or .A:17 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET16
4.310
GLU17
4.755
GLY43
3.433
ARG44
2.631
HIS45
2.997
THR46
2.799
LEU62
3.219
SER63
2.500
SER64
2.793
GLN65
4.350
VAL75
4.833
Residue
Distance (Å)
LYS76
3.277
SER77
3.931
VAL78
3.806
GLY95
3.925
GLY96
2.964
GLY97
3.210
ARG98
3.120
VAL99
3.435
GLN102
2.637
ASP122
3.075
THR123
3.566
PDB ID: 5Z6L      High-pressure Crystal Structure Analysis of M20 loop closed DHFR at 650 MPa
Method X-ray diffraction Resolution 1.90 Å Mutation No [12]
PDB Sequence
HMISLIAALA
9
VDRVIGMENA
19
MPWNLPADLA
29
WFKRNTLNKP
39
VIMGRHTWES
49

IGRPLPGRKN
59
IILSSQPGTD
69
DRVTWVKSVD
79
EAIAACGDVP
89
EIMVIGGGRV
99

YEQFLPKAQK
109
LYLTHIDAEV
119
EGDTHFPDYE
129
PDDWESVFSE
139
FHDADAQNSH
149

SYFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:49 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.531
ALA6
3.239
ALA7
2.847
ILE14
2.942
GLY15
3.415
MET16
3.988
GLU17
4.898
ASN18
3.403
ALA19
3.752
MET20
4.153
TRP22
4.203
GLY43
3.169
ARG44
2.498
HIS45
3.161
THR46
2.787
SER49
4.410
Residue
Distance (Å)
LEU62
3.042
SER63
2.706
SER64
2.700
GLN65
2.798
LYS76
3.045
SER77
4.022
VAL78
3.953
ILE94
3.070
GLY95
3.715
GLY96
2.928
GLY97
2.988
ARG98
2.884
VAL99
3.341
TYR100
2.991
GLN102
2.546
THR123
3.799
PDB ID: 5Z6M      High-pressure Crystal Structure Analysis of M20 loop closed DHFR at 800 MPa
Method X-ray diffraction Resolution 2.20 Å Mutation No [12]
PDB Sequence
HMISLIAALA
9
VDRVIGMENA
19
MPWNLPADLA
29
WFKRNTLNKP
39
VIMGRHTWES
49

IGRPLPGRKN
59
IILSSQPGTD
69
DRVTWVKSVD
79
EAIAACGDVP
89
EIMVIGGGRV
99

YEQFLPKAQK
109
LYLTHIDAEV
119
EGDTHFPDYE
129
PDDWESVFSE
139
FHDADAQNSH
149

SYFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:15 or .A:16 or .A:17 or .A:18 or .A:19 or .A:20 or .A:22 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:94 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
4.558
ALA6
3.164
ALA7
2.745
ILE14
2.794
GLY15
3.272
MET16
4.080
GLU17
4.964
ASN18
3.124
ALA19
3.001
MET20
4.134
TRP22
3.228
GLY43
3.020
ARG44
2.639
HIS45
2.713
THR46
2.805
LEU62
2.950
Residue
Distance (Å)
SER63
2.826
SER64
2.596
GLN65
2.535
VAL75
4.924
LYS76
3.033
SER77
4.183
VAL78
4.101
ILE94
3.267
GLY95
3.806
GLY96
2.931
GLY97
2.976
ARG98
2.997
VAL99
3.458
TYR100
2.784
GLN102
2.729
THR123
3.775
PDB ID: 5UII      structure of DHFR with bound buformin and NADP
Method X-ray diffraction Resolution 1.35 Å Mutation Yes [13]
PDB Sequence
GISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YSFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:14 or .A:15 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE14
4.791
GLY15
4.713
GLY43
2.649
ARG44
2.034
HIS45
2.216
THR46
1.890
TRP47
4.702
LEU62
2.320
SER63
1.777
SER64
1.880
GLN65
3.795
VAL75
4.417
Residue
Distance (Å)
LYS76
2.948
SER77
3.024
VAL78
2.838
GLY95
4.004
GLY96
2.173
GLY97
2.164
ARG98
2.049
VAL99
2.566
TYR100
4.872
GLN102
2.026
ASP122
4.940
THR123
2.733
PDB ID: 5UIP      structure of DHFR with bound DAP, p-ABG and NADP
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [13]
PDB Sequence
GISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YSFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:16 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET16
4.886
GLY43
3.427
ARG44
2.731
HIS45
3.377
THR46
2.602
LEU62
3.166
SER63
2.640
SER64
2.676
GLN65
4.376
VAL75
4.893
LYS76
3.427
Residue
Distance (Å)
SER77
4.063
VAL78
4.021
GLY95
4.057
GLY96
3.030
GLY97
3.036
ARG98
3.076
VAL99
3.445
GLN102
2.826
ASP122
4.916
THR123
3.879
PDB ID: 5UIH      structure of DHFR with bound phenformin and NADP
Method X-ray diffraction Resolution 1.65 Å Mutation No [13]
PDB Sequence
MISLIAALAV
10
DRVIGMENAM
20
PWNLPADLAW
30
FKRNTLNKPV
40
IMGRHTWESI
50

GRPLPGRKNI
60
ILSSQPGTDD
70
RVTWVKSVDE
80
AIAACGDVPE
90
IMVIGGGRVY
100

EQFLPKAQKL
110
YLTHIDAEVE
120
GDTHFPDYEP
130
DDWESVFSEF
140
HDADAQNSHS
150

YCFEILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:14 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE14
4.837
GLY43
3.445
ARG44
2.796
HIS45
3.380
THR46
2.714
LEU62
3.213
SER63
2.709
SER64
2.756
GLN65
4.380
VAL75
4.760
LYS76
3.259
Residue
Distance (Å)
SER77
3.878
VAL78
3.950
GLY95
4.045
GLY96
3.075
GLY97
2.780
ARG98
3.030
VAL99
3.396
GLN102
2.797
ASP122
4.515
THR123
2.938
PDB ID: 5UIO      structure of DHFR with bound DAP, p-ABG and NADP
Method X-ray diffraction Resolution 1.93 Å Mutation No [13]
PDB Sequence
MMISLIAALA
9
VDRVIGMENA
19
MPWNLPADLA
29
WFKRNTLNKP
39
VIMGRHTWES
49

IGRPLPGRKN
59
IILSSQPGTD
69
DRVTWVKSVD
79
EAIAACGDVP
89
EIMVIGGGRV
99

YEQFLPKAQK
109
LYLTHIDAEV
119
EGDTHFPDYE
129
PDDWESVFSE
139
FHDADAQNSH
149

SYCFEILERR
159
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAP or .NAP2 or .NAP3 or :3NAP;style chemicals stick;color identity;select .A:16 or .A:17 or .A:43 or .A:44 or .A:45 or .A:46 or .A:62 or .A:63 or .A:64 or .A:65 or .A:75 or .A:76 or .A:77 or .A:78 or .A:95 or .A:96 or .A:97 or .A:98 or .A:99 or .A:102 or .A:122 or .A:123; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET16
3.650
GLU17
3.848
GLY43
3.525
ARG44
2.689
HIS45
3.211
THR46
2.680
LEU62
3.211
SER63
2.692
SER64
2.577
GLN65
4.301
VAL75
4.959
Residue
Distance (Å)
LYS76
3.262
SER77
4.035
VAL78
4.030
GLY95
3.955
GLY96
2.874
GLY97
2.942
ARG98
2.837
VAL99
3.398
GLN102
2.889
ASP122
2.880
THR123
3.361
References  Top
REF 1 Automated identification of functional dynamic contact networks from X-ray crystallography. Nat Methods. 2013 Sep;10(9):896-902.
REF 2 Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR. Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):E445-54.
REF 3 Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway. J Am Chem Soc. 2015 Jul 29;137(29):9459-68.
REF 4 Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 1997 Jan 21;36(3):586-603.
REF 5 Capturing the Catalytic Proton of Dihydrofolate Reductase: Implications for General Acid-Base Catalysis. doi:10.1021/acscatal.1c00417.
REF 6 Native SAD phasing at room temperature. Acta Crystallogr D Struct Biol. 2022 Aug 1;78(Pt 8):986-996.
REF 7 A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis. Science. 2011 Apr 8;332(6026):234-8.
REF 8 Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications. Biochemistry. 1995 Feb 28;34(8):2710-23.
REF 9 Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry. 1990 Apr 3;29(13):3263-77.
REF 10 Mechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihydrofolate reductase of Escherichia coli. Biochim Biophys Acta. 2013 Oct;1834(10):2147-57.
REF 11 Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens. Commun Biol. 2022 May 13;5(1):459.
REF 12 High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP(). Acta Crystallogr D Struct Biol. 2018 Sep 1;74(Pt 9):895-905.
REF 13 A Structural Basis for Biguanide Activity. Biochemistry. 2017 Sep 12;56(36):4786-4798.

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