Binding Site Information of Target

Content Navigation (  All   None )                                      
Target 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
Drug Binding Sites of Target  Top
Ligand Name: Folic acid Ligand Info
Structure Description Cryogenic WT DHFR PDB:4KJJ
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
1.855
ALA6
2.709
ALA7
2.405
MET20
2.590
TRP22
3.992
PRO25
4.529
ASP27
1.977
LEU28
2.004
ALA29
2.740
TRP30
2.851
PHE31
2.458
LYS32
2.122
THR35
4.768
LEU36
4.994
Residue
Distance (Å)
THR46
2.987
SER49
4.703
ILE50
2.251
LEU54
2.723
PRO55
3.366
ARG57
1.858
ILE94
2.256
GLY95
4.366
TYR100
3.362
TYR111
4.369
LEU112
4.598
THR113
2.401
PHE153
4.255
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Methotrexate Ligand Info
Structure Description Crystal structure of the ternary MTX NADPH complex of Escherichia coli dihydrofolate reductase PDB:3DAU
Method X-ray diffraction Resolution 1.50 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
2.818
ALA6
3.422
ALA7
3.773
MET20
2.890
PRO25
3.409
ASP27
2.659
LEU28
3.449
ALA29
3.530
TRP30
4.141
PHE31
3.416
LYS32
3.324
THR35
4.875
Residue
Distance (Å)
THR46
4.132
SER49
3.927
ILE50
3.543
ARG52
2.941
LEU54
3.665
PRO55
4.211
ARG57
2.754
VAL93
4.982
ILE94
2.915
GLY95
4.713
TYR100
3.235
THR113
3.528
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Levoleucovorin Ligand Info
Structure Description THE CRYSTAL STRUCTURE OF THE BINARY COMPLEX BETWEEN FOLINIC ACID (LEUCOVORIN) AND E. COLI DIHYDROFOLATE REDUCTASE PDB:1JOM
Method X-ray diffraction Resolution 1.90 Å Mutation No [3]
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 .FFO or .FFO2 or .FFO3 or :3FFO;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:15 or .A:16 or .A:17 or .A:20 or .A:22 or .A:27 or .A:28 or .A:30 or .A:31 or .A:32 or .A:35 or .A:50 or .A:54 or .A:55 or .A:57 or .A:94 or .A:100 or .A:113; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
3.210
ALA6
3.538
ALA7
3.551
GLY15
3.524
MET16
4.487
GLU17
3.514
MET20
4.925
TRP22
4.818
ASP27
2.586
LEU28
3.823
TRP30
4.037
Residue
Distance (Å)
PHE31
3.361
LYS32
3.727
THR35
4.955
ILE50
3.878
LEU54
3.987
PRO55
4.076
ARG57
2.873
ILE94
3.407
TYR100
3.358
THR113
3.548
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Urea Ligand Info
Structure Description MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE AND UREA PDB:1DDR
Method X-ray diffraction Resolution 2.45 Å Mutation No [4]
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 .URE or .URE2 or .URE3 or :3URE;style chemicals stick;color identity;select .A:44 or .A:45 or .A:52 or .A:62 or .A:63 or .A:64 or .A:65 or .A:76 or .A:77 or .A:102; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ARG44
3.478
HIS45
3.911
ARG52
3.020
LEU62
4.878
SER63
2.922
Residue
Distance (Å)
SER64
3.784
GLN65
3.100
LYS76
3.383
SER77
4.057
GLN102
4.236
Ligand Name: Arginine Ligand Info
Structure Description Crystal structure of Escherichia coli dihydrofolate reductase in complex with TRIMETHOPRIM and NADPH PDB:7MYM
Method X-ray diffraction Resolution 3.04 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

YCFEILER
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ARG or .ARG2 or .ARG3 or :3ARG;style chemicals stick;color identity;select .A:130 or .A:131 or .A:132 or .A:133 or .A:134 or .A:157 or .A:158; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
PRO130
3.643
ASP131
2.788
ASP132
2.611
TRP133
3.027
Residue
Distance (Å)
GLU134
3.683
GLU157
4.438
ARG158
2.705
Ligand Name: Trimethoprim Ligand Info
Structure Description Crystal structure of GFP-LAMA-G97 - a GFP enhancer nanobody with cpDHFR insertion and TMP and NADPH PDB:6RUM
Method X-ray diffraction Resolution 1.60 Å Mutation No [6]
PDB Sequence
QVQLVESGGA
10
LVQPGGSLRL
20
SCAASGFPVN
30
RYSMRWYRQA
40
PGKEREWVAG
50

MSSAGDRSSY
59
EDSVKGRFTI
69
SRDDARNTVY
79
LQMNSLKPED
86
TAVYYCNVNV
96

GLPADLAWFK
106
RNTLNKPVIM
116
GRHTWESIGR
126
PLPGRKNIIL
136
SSQPGTDDRV
146

TWVKSVDEAI
156
AACGDVPEIM
166
VIGGGRVYEQ
176
FLPKAQKLYL
186
THIDAEVEGD
196

THFPDYEPDD
206
WESVFSEFHD
216
ADAQNSHSYC
226
FEILERRGGG
238
MISLIAALAV
248

DRVIGMENAM
258
PWNFEYWGQG
268
TQVTVS
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TOP or .TOP2 or .TOP3 or :3TOP;style chemicals stick;color identity;select .A:95 or .A:101 or .A:102 or .A:104 or .A:105 or .A:120 or .A:123 or .A:124 or .A:126 or .A:128 or .A:167 or .A:168 or .A:169 or .A:174 or .A:187 or .A:243 or .A:244 or .A:245 or .A:258 or .A:261; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASN95
3.788
ASP101
2.796
LEU102
4.068
TRP104
4.331
PHE105
3.343
THR120
4.968
SER123
3.553
ILE124
3.731
ARG126
4.001
LEU128
4.133
Residue
Distance (Å)
VAL167
4.954
ILE168
2.825
GLY169
4.602
TYR174
3.312
THR187
3.736
ILE243
2.860
ALA244
3.573
ALA245
3.610
MET258
3.421
ASN261
3.840
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: NADP+ Ligand Info
Structure Description Cryogenic WT DHFR PDB:4KJJ
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
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:42 or .A:43 or .A:44 or .A:45 or .A:46 or .A:47 or .A:49 or .A:50 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 #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: NADPH Ligand Info
Structure Description L28F E.coli DHFR in complex with NADPH PDB:5W3Q
Method X-ray diffraction Resolution 1.40 Å Mutation Yes [7]
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
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NDP or .NDP2 or .NDP3 or :3NDP;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: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
4.220
ALA6
2.686
ALA7
1.966
LEU8
4.126
VAL13
4.901
ILE14
1.970
GLY15
2.378
MET16
3.499
GLU17
4.079
ASN18
2.094
ALA19
2.973
MET20
2.538
PRO21
4.868
TRP22
2.471
GLY43
2.625
ARG44
1.867
HIS45
2.195
THR46
1.940
TRP47
4.797
Residue
Distance (Å)
SER49
3.984
LEU62
2.159
SER63
1.829
SER64
1.968
GLN65
3.721
VAL75
4.520
LYS76
2.881
SER77
2.921
VAL78
2.788
ILE94
2.376
GLY95
2.507
GLY96
2.264
GLY97
2.483
ARG98
2.081
VAL99
2.543
TYR100
2.358
GLN102
1.840
ASP122
3.939
THR123
2.162
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 3-Sulfinoalanine Ligand Info
Structure Description E. coli DHFR by Native Mn,P,S-SAD at Room Temperature PDB:7LVC
Method X-ray diffraction Resolution 1.70 Å Mutation No [8]
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 .CSD or .CSD2 or .CSD3 or :3CSD;style chemicals stick;color identity;select .A:112 or .A:113 or .A:114 or .A:115 or .A:138 or .A:139 or .A:140 or .A:141 or .A:150 or .A:151 or .A:153 or .A:154; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU112
3.588
THR113
2.410
HIS114
1.956
ILE115
3.966
SER138
2.439
GLU139
2.452
Residue
Distance (Å)
PHE140
2.418
HIS141
3.480
SER150
4.658
TYR151
1.322
PHE153
1.325
GLU154
3.474
Ligand Name: 2'-Monophosphoadenosine-5'-Diphosphate Ligand Info
Structure Description DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE AND 2-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE PDB:1RA8
Method X-ray diffraction Resolution 1.80 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 .ATR or .ATR2 or .ATR3 or :3ATR;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
3.432
ARG44
2.662
HIS45
2.967
THR46
2.924
LEU62
3.224
SER63
2.251
SER64
2.704
GLN65
4.276
VAL75
4.945
LYS76
3.323
Residue
Distance (Å)
SER77
4.047
VAL78
3.970
GLY95
3.979
GLY96
3.048
GLY97
2.993
ARG98
3.056
VAL99
3.379
GLN102
2.880
THR123
3.776
Ligand Name: Tellurium Ligand Info
Structure Description EXPRESSION, CHARACTERIZATION, AND CRYSTALLOGRAPHIC ANALYSIS OF TELLUROMETHIONYL DIHYDROFOLATE REDUCTASE PDB:1TDR
Method X-ray diffraction Resolution 2.50 Å Mutation No [10]
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

YCFKILERR
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TE or .TE2 or .TE3 or :3TE;style chemicals stick;color identity;select .A:3 or .A:34 or .A:38 or .A:42 or .A:43 or .A:46 or .A:47 or .A:50 or .A:61 or .A:90 or .A:91 or .A:92 or .A:94 or .A:111; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER3
3.853
ASN34
3.937
LYS38
3.894
MET42
0.471
GLY43
4.704
THR46
4.541
TRP47
3.900
Residue
Distance (Å)
ILE50
3.789
ILE61
4.087
GLU90
3.654
ILE91
4.307
MET92
0.490
ILE94
4.179
TYR111
4.191
Ligand Name: S,S-(2-Hydroxyethyl)Thiocysteine Ligand Info
Structure Description High-pressure Crystal Structure Analysis of DHFR(0.1 MPa) PDB:5Z6F
Method X-ray diffraction Resolution 1.80 Å Mutation No [11]
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 .CME or .CME2 or .CME3 or :3CME;style chemicals stick;color identity;select .A:112 or .A:113 or .A:114 or .A:138 or .A:139 or .A:140 or .A:141 or .A:150 or .A:151 or .A:153 or .A:154; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU112
3.670
THR113
3.357
HIS114
2.910
SER138
3.350
GLU139
3.315
PHE140
3.907
Residue
Distance (Å)
HIS141
4.762
SER150
4.721
TYR151
1.331
PHE153
1.335
GLU154
3.459
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: (6s)-5,6,7,8-Tetrahydrofolate Ligand Info
Structure Description E. coli DHFR complex with a reaction intermediate PDB:6MR9
Method X-ray diffraction Resolution 1.35 Å Mutation No [12]
PDB Sequence
MISLIAALAV
10
DRVIGMMPWN
23
LPADLAWFKR
33
NTLNKPVIMG
43
RHTWESIGRP
53

LPGRKNIILS
63
SQPGTDDRVT
73
WVKSVDEAIA
83
ACGDVPEIMV
93
IGGGRVYEQF
103

LPKAQKLYLT
113
HIDAEVEGDT
123
HFPDYEPDDW
133
ESVFSEFHDA
143
DAQNSHSYCF
153

EILERRHHH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .THG or .THG2 or .THG3 or :3THG;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:15 or .A:16 or .A:20 or .A:22 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:35 or .A:46 or .A:50 or .A:54 or .A:55 or .A:57 or .A:94 or .A:95 or .A:100 or .A:111 or .A:112 or .A:113 or .A:153; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.323
ALA6
2.617
ALA7
2.679
GLY15
3.849
MET16
2.954
MET20
3.658
TRP22
4.194
ASP27
1.776
LEU28
2.168
ALA29
4.667
TRP30
2.563
PHE31
2.583
LYS32
2.744
Residue
Distance (Å)
THR35
4.357
THR46
2.763
ILE50
2.846
LEU54
3.056
PRO55
3.211
ARG57
1.797
ILE94
2.301
GLY95
3.762
TYR100
2.546
TYR111
4.658
LEU112
4.843
THR113
2.827
PHE153
4.524
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Dihydrofolic acid Ligand Info
Structure Description E. coli DHFR complex modeled with two ligand states PDB:6MT8
Method X-ray diffraction Resolution 1.35 Å Mutation No [12]
PDB Sequence
MISLIAALAV
10
DRVIGMMPWN
23
LPADLAWFKR
33
NTLNKPVIMG
43
RHTWESIGRP
53

LPGRKNIILS
63
SQPGTDDRVT
73
WVKSVDEAIA
83
ACGDVPEIMV
93
IGGGRVYEQF
103

LPKAQKLYLT
113
HIDAEVEGDT
123
HFPDYEPDDW
133
ESVFSEFHDA
143
DAQNSHSYCF
153

EILERRHHH
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .DHF or .DHF2 or .DHF3 or :3DHF;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:15 or .A:16 or .A:20 or .A:22 or .A:25 or .A:27 or .A:28 or .A:30 or .A:31 or .A:32 or .A:35 or .A:46 or .A:49 or .A:50 or .A:54 or .A:55 or .A:57 or .A:94 or .A:95 or .A:100 or .A:111 or .A:112 or .A:113 or .A:153; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.063
ALA6
2.811
ALA7
2.597
GLY15
4.002
MET16
2.445
MET20
4.142
TRP22
4.203
PRO25
4.885
ASP27
2.125
LEU28
2.410
TRP30
2.577
PHE31
2.523
LYS32
2.847
THR35
4.354
Residue
Distance (Å)
THR46
2.835
SER49
4.970
ILE50
2.877
LEU54
2.891
PRO55
3.236
ARG57
1.887
ILE94
2.006
GLY95
3.874
TYR100
2.759
TYR111
4.457
LEU112
4.562
THR113
2.594
PHE153
4.386
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Phenformin Ligand Info
Structure Description structure of DHFR with bound phenformin and NADP PDB:5UIH
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 .8CV or .8CV2 or .8CV3 or :38CV;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:15 or .A:16 or .A:22 or .A:27 or .A:28 or .A:30 or .A:31 or .A:50 or .A:54 or .A:94 or .A:95 or .A:100 or .A:113; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.890
ALA6
3.737
ALA7
3.732
GLY15
4.706
MET16
3.531
TRP22
4.486
ASP27
2.768
LEU28
3.515
Residue
Distance (Å)
TRP30
4.415
PHE31
3.387
ILE50
4.072
LEU54
4.189
ILE94
3.015
GLY95
4.836
TYR100
3.287
THR113
3.779
Ligand Name: 5,10-Dideazatetrahydrofolic acid Ligand Info
Structure Description L28F E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate PDB:5CC9
Method X-ray diffraction Resolution 1.20 Å Mutation Yes [14]
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
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .DDF or .DDF2 or .DDF3 or :3DDF;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:15 or .A:20 or .A:22 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:35 or .A:36 or .A:46 or .A:50 or .A:54 or .A:55 or .A:57 or .A:94 or .A:95 or .A:100 or .A:111 or .A:113 or .A:153; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
1.902
ALA6
2.604
ALA7
2.604
GLY15
4.415
MET20
4.820
TRP22
3.666
ASP27
2.017
PHE28
2.083
ALA29
4.666
TRP30
2.596
PHE31
2.562
LYS32
2.536
THR35
4.417
Residue
Distance (Å)
LEU36
4.515
THR46
3.833
ILE50
1.988
LEU54
2.946
PRO55
3.558
ARG57
1.673
ILE94
2.199
GLY95
4.097
TYR100
2.795
TYR111
4.724
THR113
2.461
PHE153
4.347
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Deuterium Oxide Ligand Info
Structure Description Neutron crystal Structure of E.coli Dihydrofolate Reductase complexed with folate and NADP+ PDB:4PDJ
Method X-ray diffraction Resolution 1.60 Å Mutation No [15]
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 .DOD or .DOD2 or .DOD3 or :3DOD;style chemicals stick;color identity;select .A:1 or .A:2 or .A:3 or .A:5 or .A:6 or .A:7 or .A:8 or .A:9 or .A:10 or .A:11 or .A:12 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:23 or .A:24 or .A:25 or .A:26 or .A:27 or .A:28 or .A:29 or .A:30 or .A:32 or .A:33 or .A:34 or .A:35 or .A:36 or .A:37 or .A:38 or .A:39 or .A:44 or .A:45 or .A:46 or .A:47 or .A:48 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:54 or .A:55 or .A:56 or .A:57 or .A:58 or .A:59 or .A:61 or .A:62 or .A:63 or .A:64 or .A:65 or .A:66 or .A:67 or .A:68 or .A:69 or .A:70 or .A:71 or .A:72 or .A:73 or .A:74 or .A:75 or .A:76 or .A:77 or .A:78 or .A:79 or .A:80 or .A:82 or .A:83 or .A:84 or .A:85 or .A:86 or .A:87 or .A:88 or .A:89 or .A:90 or .A:91 or .A:92 or .A:97 or .A:98 or .A:100 or .A:101 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:108 or .A:109 or .A:111 or .A:112 or .A:113 or .A:114 or .A:115 or .A:116 or .A:117 or .A:118 or .A:119 or .A:120 or .A:121 or .A:122 or .A:123 or .A:124 or .A:125 or .A:126 or .A:127 or .A:128 or .A:129 or .A:130 or .A:131 or .A:132 or .A:133 or .A:134 or .A:135 or .A:136 or .A:138 or .A:139 or .A:140 or .A:141 or .A:142 or .A:143 or .A:144 or .A:145 or .A:146 or .A:147 or .A:148 or .A:149 or .A:150 or .A:151 or .A:152 or .A:153 or .A:154 or .A:156 or .A:157 or .A:158 or .A:159; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
MET1
1.961
ILE2
1.889
SER3
4.776
ILE5
2.429
ALA6
2.660
ALA7
3.616
LEU8
3.078
ALA9
2.388
VAL10
2.173
ASP11
1.951
ARG12
1.979
VAL13
2.357
ILE14
4.816
GLY15
3.931
MET16
2.817
GLU17
2.626
ASN18
1.788
ALA19
2.854
MET20
1.870
PRO21
4.799
TRP22
1.828
ASN23
1.795
LEU24
1.751
PRO25
2.042
ALA26
2.108
ASP27
1.663
LEU28
2.512
ALA29
2.323
TRP30
1.993
LYS32
2.090
ARG33
1.647
ASN34
1.966
THR35
3.575
LEU36
2.083
ASN37
2.637
LYS38
1.886
PRO39
2.519
ARG44
2.566
HIS45
2.706
THR46
3.473
TRP47
1.876
GLU48
1.931
SER49
1.853
ILE50
3.122
GLY51
2.147
ARG52
2.721
PRO53
2.508
LEU54
2.770
PRO55
2.611
GLY56
1.956
ARG57
2.516
LYS58
2.550
ASN59
1.828
ILE61
4.298
LEU62
4.421
SER63
2.328
SER64
2.847
GLN65
2.020
PRO66
2.056
GLY67
1.812
THR68
2.247
ASP69
1.881
ASP70
1.901
ARG71
1.879
VAL72
2.096
THR73
1.906
TRP74
1.989
VAL75
2.318
LYS76
2.303
SER77
1.775
VAL78
2.772
ASP79
2.008
Residue
Distance (Å)
GLU80
1.928
ILE82
1.800
ALA83
2.690
ALA84
4.874
CYS85
2.597
GLY86
2.058
ASP87
2.953
VAL88
1.970
PRO89
2.400
GLU90
2.037
ILE91
2.789
MET92
4.657
GLY97
2.999
ARG98
1.717
TYR100
4.031
GLU101
2.120
GLN102
2.026
PHE103
4.132
LEU104
2.527
PRO105
2.200
LYS106
2.353
ALA107
3.078
GLN108
1.747
LYS109
1.847
TYR111
2.084
LEU112
2.827
THR113
2.158
HIS114
1.658
ILE115
2.356
ASP116
1.549
ALA117
3.824
GLU118
2.297
VAL119
1.785
GLU120
1.979
GLY121
4.790
ASP122
1.984
THR123
2.318
HIS124
1.949
PHE125
2.974
PRO126
2.304
ASP127
4.830
TYR128
2.239
GLU129
1.758
PRO130
2.053
ASP131
2.031
ASP132
2.794
TRP133
2.071
GLU134
2.746
SER135
1.873
VAL136
3.112
SER138
1.741
GLU139
3.039
PHE140
1.984
HIS141
1.742
ASP142
1.954
ALA143
1.887
ASP144
2.304
ALA145
4.040
GLN146
2.140
ASN147
2.732
SER148
2.040
HIS149
2.420
SER150
1.926
TYR151
1.902
CYS152
2.806
PHE153
2.951
GLU154
2.005
LEU156
2.904
GLU157
1.579
ARG158
2.218
ARG159
2.233
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: (2s,2's)-5,5'-(Nonane-1,9-Diyldiimino)bis(2-{[(4-{[(2,4-Diaminopteridin-6-Yl)methyl](Methyl)amino}phenyl)carbonyl]amino}-5-Oxopentanoic Acid) (Non-Preferred Name) Ligand Info
Structure Description Chemically Self-assembled Antibody Nanorings (CSANs): Design and Characterization of an Anti-CD3 IgM Biomimetic PDB:3OCH
Method X-ray diffraction Resolution 1.79 Å Mutation No [16]
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 .2MX or .2MX2 or .2MX3 or :32MX;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:27 or .A:28 or .A:30 or .A:31 or .A:32 or .A:35 or .A:46 or .A:49 or .A:50 or .A:52 or .A:54 or .A:55 or .A:57 or .A:94 or .A:95 or .A:100 or .A:113; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.823
ALA6
3.474
ALA7
3.639
ASP27
2.593
LEU28
3.549
TRP30
4.023
PHE31
3.374
LYS32
3.364
THR35
4.842
THR46
4.154
Residue
Distance (Å)
SER49
3.716
ILE50
3.470
ARG52
2.967
LEU54
3.717
PRO55
4.511
ARG57
2.690
ILE94
2.891
GLY95
4.812
TYR100
3.541
THR113
3.370
Ligand Name: (7s)-7-Methyl-5,6,7,8-Tetrahydroquinazoline-2,4-Diamine Ligand Info
Structure Description Sensitivity of receptor internal motions to ligand binding affinity and kinetic off-rate PDB:3QYL
Method X-ray diffraction Resolution 1.79 Å Mutation No [17]
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 .7ME or .7ME2 or .7ME3 or :37ME;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:20 or .A:27 or .A:28 or .A:30 or .A:31 or .A:50 or .A:94 or .A:95 or .A:100 or .A:113; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.921
ALA6
3.620
ALA7
3.779
MET20
3.534
ASP27
2.752
LEU28
3.630
TRP30
4.302
Residue
Distance (Å)
PHE31
3.426
ILE50
4.188
ILE94
2.852
GLY95
4.727
TYR100
3.402
THR113
3.696
Ligand Name: 5-Deazafolic acid Ligand Info
Structure Description ISOMORPHOUS CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE, 5-DEAZAFOLATE AND 5,10-DIDEAZATETRAHYDROFOLATE: MECHANISTIC IMPLICATIONS PDB:1DYH
Method X-ray diffraction Resolution 1.90 Å Mutation No [18]
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 .DZF or .DZF2 or .DZF3 or :3DZF;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:35 or .A:46 or .A:49 or .A:50 or .A:52 or .A:54 or .A:55 or .A:57 or .A:94 or .A:100 or .A:113; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
3.523
ALA6
3.540
ALA7
3.642
ASP27
2.630
LEU28
3.427
ALA29
4.142
TRP30
4.025
PHE31
3.225
LYS32
3.769
THR35
4.887
Residue
Distance (Å)
THR46
3.509
SER49
4.885
ILE50
3.571
ARG52
3.200
LEU54
3.768
PRO55
4.301
ARG57
2.615
ILE94
3.037
TYR100
3.761
THR113
3.432
Ligand Name: 5-[(4-Chlorophenyl)sulfanyl]quinazoline-2,4-Diamine Ligand Info
Structure Description Dynamic switching and partial occupancies of a small molecule inhibitor complex of DHFR PDB:3KFY
Method X-ray diffraction Resolution 2.08 Å Mutation Yes [19]
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 .JZM or .JZM2 or .JZM3 or :3JZM;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:14 or .A:20 or .A:27 or .A:28 or .A:30 or .A:31 or .A:46 or .A:94 or .A:95 or .A:96 or .A:97 or .A:100 or .A:113; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
3.102
ALA6
3.822
ALA7
3.809
ILE14
3.442
MET20
3.252
ASP27
2.189
LEU28
3.526
TRP30
4.058
Residue
Distance (Å)
PHE31
3.259
THR46
4.342
ILE94
1.717
GLY95
3.229
GLY96
3.376
GLY97
4.185
TYR100
2.491
THR113
3.323
Ligand Name: (6s)-6-Methyl-5,6,7,8-Tetrahydroquinazoline-2,4-Diamine Ligand Info
Structure Description Evidence for dynamic motion in proteins as a mechanism for ligand dissociation PDB:3R33
Method X-ray diffraction Resolution 2.09 Å Mutation No [17]
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 .6ME or .6ME2 or .6ME3 or :36ME;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:20 or .A:27 or .A:28 or .A:30 or .A:31 or .A:46 or .A:50 or .A:94 or .A:95 or .A:100 or .A:113; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.916
ALA6
3.479
ALA7
3.836
MET20
4.010
ASP27
2.670
LEU28
3.725
TRP30
4.135
Residue
Distance (Å)
PHE31
3.468
THR46
4.828
ILE50
3.777
ILE94
2.881
GLY95
4.701
TYR100
3.181
THR113
3.653
Ligand Name: Quinazoline-2,4-diamine Ligand Info
Structure Description Sensitivity of receptor internal motions to ligand binding affinity and kinetic off-rate PDB:3QYO
Method X-ray diffraction Resolution 2.09 Å Mutation No [17]
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 .Q24 or .Q242 or .Q243 or :3Q24;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:20 or .A:27 or .A:28 or .A:30 or .A:31 or .A:50 or .A:94 or .A:95 or .A:100 or .A:113; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.897
ALA6
3.546
ALA7
3.769
MET20
3.479
ASP27
2.682
LEU28
3.528
TRP30
4.203
Residue
Distance (Å)
PHE31
3.363
ILE50
4.431
ILE94
3.012
GLY95
4.864
TYR100
3.354
THR113
3.692
Ligand Name: (2,5-Dimethylbenzene-1,4-Diyl)dimethanediyl Bis(N-Carbamimidoylcarbamimidothioate) Ligand Info
Structure Description Crystal Structure of E.coli DHFR in complex with NADPH and the inhibitor compound 10a. PDB:2ANQ
Method X-ray diffraction Resolution 2.13 Å Mutation Yes [20]
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 .C1A or .C1A2 or .C1A3 or :3C1A;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:18 or .A:19 or .A:20 or .A:27 or .A:28 or .A:30 or .A:31 or .A:46 or .A:49 or .A:50 or .A:94 or .A:95 or .A:100 or .A:113; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
3.070
ALA6
3.670
ALA7
3.783
ASN18
4.567
ALA19
3.386
MET20
3.518
ASP27
2.916
LEU28
4.423
TRP30
4.539
Residue
Distance (Å)
PHE31
3.388
THR46
3.985
SER49
3.717
ILE50
3.747
ILE94
3.020
GLY95
4.844
TYR100
3.440
THR113
3.934
Ligand Name: N-(4-{[(2,4-Diaminopteridin-1-Ium-6-Yl)methyl](Methyl)amino}benzoyl)-L-Glutamic Acid Ligand Info
Structure Description Neutron Crystal Structure of Escherichia coli Dihydrofolate Reductase Bound to the Anti-cancer drug, Methotrexate PDB:2INQ
Method Neutron diffraction Resolution 2.20 Å Mutation Yes [21]
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 .MT1 or .MT12 or .MT13 or :3MT1;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:27 or .A:28 or .A:29 or .A:30 or .A:31 or .A:32 or .A:35 or .A:46 or .A:49 or .A:50 or .A:52 or .A:54 or .A:55 or .A:57 or .A:93 or .A:94 or .A:95 or .A:100 or .A:111 or .A:112 or .A:113 or .A:153; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
1.475
ALA6
2.207
ALA7
2.799
ASP27
1.757
LEU28
2.432
ALA29
4.310
TRP30
3.185
PHE31
2.343
LYS32
2.920
THR35
4.647
THR46
2.232
SER49
2.606
ILE50
2.609
Residue
Distance (Å)
ARG52
4.129
LEU54
3.010
PRO55
3.372
ARG57
1.777
VAL93
4.449
ILE94
2.024
GLY95
4.652
TYR100
2.726
TYR111
3.941
LEU112
4.046
THR113
3.322
PHE153
4.897
Ligand Name: 1-{[N-(1-Imino-guanidino-methyl)]sulfanylmethyl}-3-trifluoromethyl-benzene Ligand Info
Structure Description Crystal structure of E.coli dihydrofolate reductase in complex with NADPH and the inhibitor MS-SH08-17 PDB:2ANO
Method X-ray diffraction Resolution 2.68 Å Mutation Yes [20]
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 .817 or .8172 or .8173 or :3817;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:20 or .A:27 or .A:28 or .A:30 or .A:31 or .A:46 or .A:50 or .A:54 or .A:94 or .A:100 or .A:113; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.585
ALA6
3.267
ALA7
3.837
MET20
3.574
ASP27
2.665
LEU28
3.340
TRP30
3.659
Residue
Distance (Å)
PHE31
3.424
THR46
4.719
ILE50
3.972
LEU54
3.044
ILE94
3.962
TYR100
3.398
THR113
3.330
Ligand Name: Buformin Ligand Info
Structure Description structure of DHFR with bound buformin and NADP PDB:5UII
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 .BFR or .BFR2 or .BFR3 or :3BFR;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:27 or .A:28 or .A:30 or .A:31 or .A:46 or .A:49 or .A:50 or .A:54 or .A:93 or .A:94 or .A:95 or .A:100 or .A:111 or .A:113 or .A:153; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
1.886
ALA6
2.552
ALA7
2.734
ASP27
1.846
LEU28
4.254
TRP30
3.061
PHE31
2.885
THR46
4.122
SER49
4.516
Residue
Distance (Å)
ILE50
2.172
LEU54
2.904
VAL93
4.628
ILE94
2.027
GLY95
4.091
TYR100
2.293
TYR111
4.695
THR113
2.625
PHE153
4.697
Ligand Name: 2,4-Diaminopyrimidine Ligand Info
Structure Description structure of DHFR with bound DAP, p-ABG and NADP PDB:5UIP
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 .LG3 or .LG32 or .LG33 or :3LG3;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:27 or .A:28 or .A:30 or .A:31 or .A:94 or .A:100 or .A:113; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.987
ALA6
3.624
ALA7
3.798
ASP27
2.772
LEU28
4.243
Residue
Distance (Å)
TRP30
4.134
PHE31
3.476
ILE94
3.059
TYR100
3.434
THR113
3.540
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: N-(4-Aminobenzoyl)-L-glutamic acid Ligand Info
Structure Description structure of DHFR with bound DAP, p-ABG and NADP PDB:5UIP
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 .8DM or .8DM2 or .8DM3 or :38DM;style chemicals stick;color identity;select .A:28 or .A:31 or .A:32 or .A:35 or .A:46 or .A:50 or .A:52 or .A:54 or .A:55 or .A:57; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU28
3.753
PHE31
3.435
LYS32
3.405
THR35
4.845
THR46
4.918
Residue
Distance (Å)
ILE50
3.795
ARG52
3.925
LEU54
3.998
PRO55
4.147
ARG57
2.592
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 7-[(3-aminophenyl)methyl]-7H-pyrrolo[3,2-f]quinazoline-1,3-diamine Ligand Info
Structure Description E. coli DHFR complex with inhibitor AMPQD PDB:6CQA
Method X-ray diffraction Resolution 2.20 Å Mutation No [22]
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 .PQD or .PQD2 or .PQD3 or :3PQD;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:16 or .A:18 or .A:22 or .A:27 or .A:28 or .A:30 or .A:31 or .A:32 or .A:46 or .A:49 or .A:50 or .A:52 or .A:54 or .A:93 or .A:94 or .A:95 or .A:100 or .A:111 or .A:112 or .A:113 or .A:153; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
2.115
ALA6
2.759
ALA7
2.790
MET16
3.497
ASN18
3.197
TRP22
3.876
ASP27
1.987
LEU28
3.115
TRP30
3.137
PHE31
2.546
LYS32
3.258
THR46
2.357
Residue
Distance (Å)
SER49
3.369
ILE50
2.593
ARG52
3.679
LEU54
2.827
VAL93
4.648
ILE94
2.220
GLY95
4.230
TYR100
2.418
TYR111
4.145
LEU112
4.575
THR113
2.767
PHE153
4.718
Ligand Name: 7-[(2-Fluorophenyl)methyl]pyrrolo[3,2-f]quinazoline-1,3-diamine Ligand Info
Structure Description cocrystallization of Escherichia coli dihydrofolate reductase (DHFR) and its pyrrolo[3,2-f]quinazoline inhibitor. PDB:7F3B
Method X-ray diffraction Resolution 2.81 Å Mutation No [23]
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 .D4C or .D4C2 or .D4C3 or :3D4C;style chemicals stick;color identity;select .A:5 or .A:6 or .A:7 or .A:17 or .A:18 or .A:22 or .A:27 or .A:28 or .A:30 or .A:31 or .A:32 or .A:46 or .A:49 or .A:50 or .A:54 or .A:94 or .A:95 or .A:100 or .A:111 or .A:113; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE5
3.039
ALA6
2.986
ALA7
3.562
GLU17
2.663
ASN18
3.805
TRP22
4.125
ASP27
2.830
LEU28
3.548
TRP30
4.126
PHE31
3.215
Residue
Distance (Å)
LYS32
4.748
THR46
3.834
SER49
3.568
ILE50
3.894
LEU54
3.666
ILE94
2.824
GLY95
4.875
TYR100
3.738
TYR111
4.483
THR113
3.337
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 X-ray structure of the ternary MTX.NADPH complex of the anthrax dihydrofolate reductase: a pharmacophore for dual-site inhibitor design. J Struct Biol. 2009 May;166(2):162-71.
REF 3 Crystal structures of Escherichia coli dihydrofolate reductase complexed with 5-formyltetrahydrofolate (folinic acid) in two space groups: evidence for enolization of pteridine O4. Biochemistry. 1996 Jun 4;35(22):7012-20.
REF 4 The effect of denaturants on protein structure. Protein Sci. 1997 Aug;6(8):1727-33.
REF 5 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 6 Chemogenetic Control of Nanobodies. Nat Methods. 2020 Mar;17(3):279-282.
REF 7 Defining the Structural Basis for Allosteric Product Release from E. coli Dihydrofolate Reductase Using NMR Relaxation Dispersion. J Am Chem Soc. 2017 Aug 16;139(32):11233-11240.
REF 8 Native SAD phasing at room temperature. Acta Crystallogr D Struct Biol. 2022 Aug 1;78(Pt 8):986-996.
REF 9 Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 1997 Jan 21;36(3):586-603.
REF 10 Expression, characterization and crystallographic analysis of telluromethionyl dihydrofolate reductase. Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):731-9.
REF 11 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 12 Time-resolved x-ray crystallography capture of a slow reaction tetrahydrofolate intermediate. Struct Dyn. 2019 Mar 1;6(2):024701.
REF 13 A Structural Basis for Biguanide Activity. Biochemistry. 2017 Sep 12;56(36):4786-4798.
REF 14 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 15 Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography. Proc Natl Acad Sci U S A. 2014 Dec 23;111(51):18225-30.
REF 16 Chemically self-assembled antibody nanorings (CSANs): design and characterization of an anti-CD3 IgM biomimetic. J Am Chem Soc. 2010 Dec 8;132(48):17247-57.
REF 17 Evidence for dynamics in proteins as a mechanism for ligand dissociation. Nat Chem Biol. 2012 Jan 15;8(3):246-52.
REF 18 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 19 Dynamic switching and partial occupancies of a small molecule inhibitor complex of DHFR
REF 20 A 2.13 A structure of E. coli dihydrofolate reductase bound to a novel competitive inhibitor reveals a new binding surface involving the M20 loop region. J Med Chem. 2006 Nov 30;49(24):6977-86.
REF 21 Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate. Proc Natl Acad Sci U S A. 2006 Dec 5;103(49):18493-8.
REF 22 The crystal structure of a tetrahydrofolate-bound dihydrofolate reductase reveals the origin of slow product release. Commun Biol. 2018 Dec 12;1:226.
REF 23 The discovery of 1, 3-diamino-7H-pyrrol[3, 2-f]quinazoline compounds as potent antimicrobial antifolates. Eur J Med Chem. 2022 Jan 15;228:113979.

If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.