Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T15851 Target Info
Target Name Orotidine 5'-monophosphate decarboxylase (UMPS)
Synonyms Uridine 5'-monophosphate synthase; UMP synthase
Target Type Literature-reported Target
Gene Name UMPS
Biochemical Class Pentosyltransferase
UniProt ID
UMPS_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: 3-Sulfinoalanine Ligand Info
Structure Description Crystal structure of human orotidine-5'-monophosphate decarboxylase complexed with pyrazofurin monophosphate PDB:3MI2
Method X-ray diffraction Resolution 1.20 Å Mutation No [1]
PDB Sequence
KELSFGARAE
43
LPRIHPVASK
53
LLRLMQKKET
63
NLCLSADVSL
73
ARELLQLADA
83

LGPSICMLKT
93
HVDILNDFTL
103
DVMKELITLA
113
KHEFLIFEDR
124
KFADIGNTVK
134

KQYEGGIFKI
144
ASWADLVNAH
154
VVPGSGVVKG
164
LQEVGLPLHR
174
GCLLIAEMSS
184

TGSLATGDYT
194
RAAVRMAEEH
204
SEFVVGFISG
214
SRVSMKPEFL
224
HLTPGVQLEA
234

GGDNLGQQYN
244
SPQEVIGKRG
254
SDIIIVGRGI
264
ISAADRLEAA
274
EMYRKAAWEA
284

YLSRLG
Residue
Distance (Å)
ASP82
4.610
ILE110
4.856
THR111
2.954
LEU112
3.302
Residue
Distance (Å)
ALA113
3.472
LYS114
1.333
HIS116
1.331
GLU117
3.346
Ligand Name: Cysteine Sulfenic Acid Ligand Info
Structure Description Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified by 5-fluoro-6-iodo-UMP PDB:3G3M
Method X-ray diffraction Resolution 1.40 Å Mutation No [2]
PDB Sequence
KELSFGARAE
43
LPRIHPVASK
53
LLRLMQKKET
63
NLCLSADVSL
73
ARELLQLADA
83

LGPSICMLKT
93
HVDILNDFTL
103
DVMKELITLA
113
KHEFLIFEDR
124
KFADIGNTVK
134

KQYEGGIFKI
144
ASWADLVNAH
154
VVPGSGVVKG
164
LQEVGLPLHR
174
GCLLIAEMSS
184

TGSLATGDYT
194
RAAVRMAEEH
204
SEFVVGFISG
214
SRVSMKPEFL
224
HLTPGVQLEA
234

GGDNLGQQYN
244
SPQEVIGKRG
254
SDIIIVGRGI
264
ISAADRLEAA
274
EMYRKAAWEA
284

YLSRLG
Residue
Distance (Å)
ILE110
4.866
THR111
2.955
LEU112
3.343
ALA113
3.444
Residue
Distance (Å)
LYS114
1.336
HIS116
1.331
GLU117
3.450
Ligand Name: 6-amino-uridine monophosphate Ligand Info
Structure Description Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Complexed with 6-NH2-UMP PDB:3DBP
Method X-ray diffraction Resolution 1.50 Å Mutation No [3]
PDB Sequence
KELSFGARAE
43
LPRIHPVASK
53
LLRLMQKKET
63
NLCLSADVSL
73
ARELLQLADA
83

LGPSICMLKT
93
HVDILNDFTL
103
DVMKELITLA
113
KCHEFLIFED
123
RKFADIGNTV
133

KKQYEGGIFK
143
IASWADLVNA
153
HVVPGSGVVK
163
GLQEVGLPLH
173
RGCLLIAEMS
183

STGSLATGDY
193
TRAAVRMAEE
203
HSEFVVGFIS
213
GSRVSMKPEF
223
LHLTPGVQLE
233

AGGDNLGQQY
243
NSPQEVIGKR
253
GSDIIIVGRG
263
IISAADRLEA
273
AEMYRKAAWE
283

AYLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NUP or .NUP2 or .NUP3 or :3NUP;style chemicals stick;color identity;select .A:68 or .A:70 or .A:92 or .A:94 or .A:123 or .A:125 or .A:152 or .A:181 or .A:182 or .A:183 or .A:184 or .A:212 or .A:228 or .A:229 or .A:230 or .A:241 or .A:243 or .A:259 or .A:260 or .A:261 or .A:262 or .A:263; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.141
ASP70
2.718
LYS92
2.905
HIS94
3.022
ASP123
2.917
LYS125
2.665
ASN152
4.636
GLU181
4.178
MET182
3.120
SER183
2.813
SER184
4.861
Residue
Distance (Å)
ILE212
4.082
PRO228
3.254
GLY229
4.337
VAL230
4.302
GLN241
2.933
TYR243
2.673
ILE259
4.064
VAL260
3.929
GLY261
2.881
ARG262
2.791
GLY263
4.659
Ligand Name: Uridine-5'-Monophosphate Ligand Info
Structure Description OMPD-domain of human UMPS in complex with the substrate OMP at 0.99 Angstroms resolution PDB:7AM9
Method X-ray diffraction Resolution 0.99 Å Mutation No [4]
PDB Sequence
ELSFGARAEL
233
PRIHPVASKL
243
LRLMQKKETN
253
LCLSADVSLA
263
RELLQLADAL
273

GPSICMLKTH
283
VDILNDFTLD
293
VMKELITLAK
303
HEFLIFEDRF
315
ADIGNTVKKQ
325

YEGGIFKIAS
335
WADLVNAHVV
345
PGSGVVKGLQ
355
EVGLPLHRGC
365
LLIAEMSSTG
375

SLATGDYTRA
385
AVRMAEEHSE
395
FVVGFISGSR
405
VSMKPEFLHL
415
TPGVQLEAGG
425

DNLGQQYNSP
435
QEVIGKRGSD
445
IIIVGRGIIS
455
AADRLEAAEM
465
YRKAAWEAYL
475

SRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .U or .U2 or .U3 or :3U;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.166
ASP259
2.816
LYS281
2.759
HIS283
2.956
ASP312
3.613
GLU370
4.311
MET371
3.229
SER372
2.810
SER373
4.929
ILE401
4.033
Residue
Distance (Å)
PRO417
3.295
GLY418
4.237
VAL419
4.422
GLN430
2.863
TYR432
2.676
ILE448
3.986
VAL449
4.070
GLY450
2.992
ARG451
2.700
GLY452
4.876
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 6-aza-uridine monophosphate Ligand Info
Structure Description OMPD-domain of human UMPS in complex with 6-Aza-UMP at 1.0 Angstroms resolution PDB:6ZX1
Method X-ray diffraction Resolution 1.00 Å Mutation No [4]
PDB Sequence
ELSFGARAEL
233
PRIHPVASKL
243
LRLMQKKETN
253
LCLSADVSLA
263
RELLQLADAL
273

GPSICMLKTH
283
VDILNDFTLD
293
VMKELITLAK
303
HEFLIFEDRK
314
FADIGNTVKK
324

QYEGGIFKIA
334
SWADLVNAHV
344
VPGSGVVKGL
354
QEVGLPLHRG
364
CLLIAEMSST
374

GSLATGDYTR
384
AAVRMAEEHS
394
EFVVGFISGS
404
RVSMKPEFLH
414
LTPGVQLEAG
424

GDNLGQQYNS
434
PQEVIGKRGS
444
DIIIVGRGII
454
SAADRLEAAE
464
MYRKAAWEAY
474

LSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .UP6 or .UP62 or .UP63 or :3UP6;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:341 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.158
ASP259
2.721
LYS281
2.893
HIS283
2.974
ASP312
3.380
LYS314
2.772
ASN341
4.880
GLU370
4.517
MET371
3.203
SER372
2.823
SER373
4.578
Residue
Distance (Å)
ILE401
4.389
PRO417
3.315
GLY418
4.710
VAL419
4.471
GLN430
2.921
TYR432
2.652
ILE448
4.050
VAL449
3.984
GLY450
2.887
ARG451
2.747
GLY452
4.825
Ligand Name: S,S-(2-Hydroxyethyl)Thiocysteine Ligand Info
Structure Description K314A mutant of human orotidyl-5'-monophosphate decarboxylase soaked with OMP, decarboxylated to UMP PDB:3EWY
Method X-ray diffraction Resolution 1.10 Å Mutation Yes [5]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KHEFLIFEDR
313
AFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRLG
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:299 or .A:300 or .A:301 or .A:302 or .A:303 or .A:305 or .A:306; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE299
4.823
THR300
2.946
LEU301
3.283
ALA302
3.410
Residue
Distance (Å)
LYS303
1.325
HIS305
1.331
GLU306
3.397
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 2'-deoxyuridylic acid Ligand Info
Structure Description Crystal structure of the orotidine-5'-monophosphate decarboxylase domain of human UMP synthase bound to 5-iodo-UMP PDB:2QCH
Method X-ray diffraction Resolution 1.95 Å Mutation No [6]
PDB Sequence
ELSFGARAEL
233
PRIHPVASKL
243
LRLMQKKETN
253
LCLSADVSLA
263
RELLQLADAL
273

GPSICMLKTH
283
VDILNDFTLD
293
VMKELITLAK
303
CHEFLIFEDR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .UMP or .UMP2 or .UMP3 or :3UMP;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.488
ASP259
3.018
LYS281
2.803
HIS283
3.183
ASP312
3.834
LYS314
3.261
GLU370
4.348
MET371
3.230
SER372
2.759
SER373
4.833
ILE401
4.440
Residue
Distance (Å)
PRO417
3.542
GLY418
4.264
VAL419
4.607
GLN430
2.737
TYR432
2.643
ILE448
4.415
VAL449
3.978
GLY450
2.848
ARG451
2.785
GLY452
4.867
Ligand Name: 5-Iodo-2'-Deoxyuridine-5'-Monophosphate Ligand Info
Structure Description Crystal structure of the orotidine-5'-monophosphate decarboxylase domain of human UMP synthase bound to 5-iodo-UMP PDB:2QCH
Method X-ray diffraction Resolution 1.95 Å Mutation No [6]
PDB Sequence
ELSFGARAEL
233
PRIHPVASKL
243
LRLMQKKETN
253
LCLSADVSLA
263
RELLQLADAL
273

GPSICMLKTH
283
VDILNDFTLD
293
VMKELITLAK
303
CHEFLIFEDR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .5IU or .5IU2 or .5IU3 or :35IU;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:341 or .A:343 or .A:368 or .A:370 or .A:371 or .A:372 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.375
ASP259
2.737
LYS281
3.094
HIS283
3.561
ASP312
3.875
LYS314
2.493
ASN341
4.670
HIS343
4.772
ILE368
3.737
GLU370
4.259
MET371
3.256
SER372
3.049
Residue
Distance (Å)
ILE401
4.107
PRO417
3.404
GLY418
3.949
VAL419
4.116
GLN430
2.745
TYR432
2.628
ILE448
4.393
VAL449
4.156
GLY450
3.150
ARG451
2.643
GLY452
4.559
Ligand Name: Uridine-5'-Monophosphate Ligand Info
Structure Description Orotidine 5'-monophosphate decarboxylase-domain of human UMPS in complex with the reaction product UMP at 0.95 Angstrom resolution PDB:7ASQ
Method X-ray diffraction Resolution 0.95 Å Mutation No [4]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KHEFLIFEDR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .U5P or .U5P2 or .U5P3 or :3U5P;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:368 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:420 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
2.607
ASP259
2.718
LYS281
2.014
HIS283
3.005
ASP312
3.650
LYS314
2.493
ILE368
4.937
GLU370
4.231
MET371
2.425
SER372
2.174
SER373
4.348
ILE401
3.338
Residue
Distance (Å)
PRO417
2.837
GLY418
3.811
VAL419
4.207
GLN420
4.301
GLN430
2.082
TYR432
1.872
ILE448
3.544
VAL449
3.476
GLY450
2.074
ARG451
1.888
GLY452
3.948
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 6-Hydroxyuridine-5'-Phosphate Ligand Info
Structure Description Human OMPD-domain of UMPS in complex with 6-hydroxy-UMP at 0.9 Angstroms resolution, crystal 1 PDB:7OUZ
Method X-ray diffraction Resolution 0.90 Å Mutation No [4]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KHEFLIFEDR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BMP or .BMP2 or .BMP3 or :3BMP;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:341 or .A:368 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:420 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
2.505
ASP259
2.431
LYS281
2.037
HIS283
2.417
ASP312
2.833
LYS314
1.820
ASN341
4.389
ILE368
4.975
GLU370
4.171
MET371
2.372
SER372
1.820
SER373
4.202
Residue
Distance (Å)
ILE401
3.301
PRO417
2.705
GLY418
2.949
VAL419
4.201
GLN420
4.279
GLN430
2.071
TYR432
1.842
ILE448
3.316
VAL449
3.467
GLY450
2.063
ARG451
1.879
GLY452
3.972
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 5-Hydroxycytidine 5'-(Dihydrogen Phosphate) Ligand Info
Structure Description Crystal structure of human orotidine 5'-monophosphate decarboxylase complexed with CMP-N3-oxide PDB:4HKP
Method X-ray diffraction Resolution 1.75 Å Mutation No [7]
PDB Sequence
ELSFGARAEL
44
PRIHPVASKL
54
LRLMQKKETN
64
LCLSADVSLA
74
RELLQLADAL
84

GPSICMLKTH
94
VDILNDFTLD
104
VMKELITLAK
114
CHEFLIFEDR
124
KFADIGNTVK
134

KQYEGGIFKI
144
ASWADLVNAH
154
VVPGSGVVKG
164
LQEVGLPLHR
174
GCLLIAEMSS
184

TGSLATGDYT
194
RAAVRMAEEH
204
SEFVVGFISG
214
SRVSMKPEFL
224
HLTPGVQLEA
234

GGDNLGQQYN
244
SPQEVIGKRG
254
SDIIIVGRGI
264
ISAADRLEAA
274
EMYRKAAWEA
284

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TKW or .TKW2 or .TKW3 or :3TKW;style chemicals stick;color identity;select .A:68 or .A:70 or .A:92 or .A:94 or .A:123 or .A:125 or .A:152 or .A:179 or .A:181 or .A:182 or .A:183 or .A:212 or .A:228 or .A:229 or .A:230 or .A:231 or .A:241 or .A:243 or .A:259 or .A:260 or .A:261 or .A:262 or .A:263; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.063
ASP70
2.817
LYS92
2.730
HIS94
3.022
ASP123
3.600
LYS125
2.894
ASN152
4.878
ILE179
4.355
GLU181
4.069
MET182
3.196
SER183
2.925
ILE212
3.302
Residue
Distance (Å)
PRO228
3.380
GLY229
4.410
VAL230
4.217
GLN231
4.777
GLN241
2.779
TYR243
3.069
ILE259
4.105
VAL260
4.108
GLY261
2.983
ARG262
2.752
GLY263
4.496
Ligand Name: N-Hydroxycytidine 5'-(Dihydrogen Phosphate) Ligand Info
Structure Description Crystal structure of human orotidine 5'-monophosphate decarboxylase complexed with CMP-N3-oxide PDB:4HKP
Method X-ray diffraction Resolution 1.75 Å Mutation No [7]
PDB Sequence
ELSFGARAEL
44
PRIHPVASKL
54
LRLMQKKETN
64
LCLSADVSLA
74
RELLQLADAL
84

GPSICMLKTH
94
VDILNDFTLD
104
VMKELITLAK
114
CHEFLIFEDR
124
KFADIGNTVK
134

KQYEGGIFKI
144
ASWADLVNAH
154
VVPGSGVVKG
164
LQEVGLPLHR
174
GCLLIAEMSS
184

TGSLATGDYT
194
RAAVRMAEEH
204
SEFVVGFISG
214
SRVSMKPEFL
224
HLTPGVQLEA
234

GGDNLGQQYN
244
SPQEVIGKRG
254
SDIIIVGRGI
264
ISAADRLEAA
274
EMYRKAAWEA
284

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .16B or .16B2 or .16B3 or :316B;style chemicals stick;color identity;select .A:68 or .A:70 or .A:92 or .A:94 or .A:123 or .A:125 or .A:181 or .A:182 or .A:183 or .A:184 or .A:212 or .A:228 or .A:229 or .A:230 or .A:241 or .A:243 or .A:259 or .A:260 or .A:261 or .A:262 or .A:263; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.068
ASP70
2.643
LYS92
2.959
HIS94
2.888
ASP123
3.671
LYS125
2.972
GLU181
3.666
MET182
3.067
SER183
2.685
SER184
4.515
ILE212
4.004
Residue
Distance (Å)
PRO228
3.298
GLY229
3.807
VAL230
4.628
GLN241
2.551
TYR243
2.566
ILE259
4.109
VAL260
4.083
GLY261
2.975
ARG262
2.595
GLY263
4.776
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Xanthosine-5'-monophosphate Ligand Info
Structure Description Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Complexed with XMP PDB:3BVJ
Method X-ray diffraction Resolution 1.80 Å Mutation No [8]
PDB Sequence
KELSFGARAE
43
LPRIHPVASK
53
LLRLMQKKET
63
NLCLSADVSL
73
ARELLQLADA
83

LGPSICMLKT
93
HVDILNDFTL
103
DVMKELITLA
113
KCHEFLIFED
123
RKFADIGNTV
133

KKQYEGGIFK
143
IASWADLVNA
153
HVVPGSGVVK
163
GLQEVGLPLH
173
RGCLLIAEMS
183

STGSLATGDY
193
TRAAVRMAEE
203
HSEFVVGFIS
213
GSRVSMKPEF
223
LHLTPGVQLE
233

AGGDNLGQQY
243
NSPQEVIGKR
253
GSDIIIVGRG
263
IISAADRLEA
273
AEMYRKAAWE
283

AYLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .XMP or .XMP2 or .XMP3 or :3XMP;style chemicals stick;color identity;select .A:68 or .A:70 or .A:92 or .A:94 or .A:123 or .A:125 or .A:152 or .A:179 or .A:181 or .A:182 or .A:183 or .A:184 or .A:212 or .A:228 or .A:229 or .A:230 or .A:241 or .A:243 or .A:259 or .A:260 or .A:261 or .A:262 or .A:263; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.203
ASP70
2.709
LYS92
2.898
HIS94
2.924
ASP123
3.925
LYS125
2.882
ASN152
3.648
ILE179
3.714
GLU181
4.078
MET182
3.056
SER183
2.768
SER184
4.765
Residue
Distance (Å)
ILE212
3.401
PRO228
3.237
GLY229
4.509
VAL230
4.472
GLN241
3.052
TYR243
2.728
ILE259
4.098
VAL260
4.066
GLY261
2.952
ARG262
2.705
GLY263
4.837
Ligand Name: (1s)-1,4-Anhydro-1-(5-Carbamoyl-4-Hydroxy-1h-Pyrazol-3-Yl)-5-O-Phosphono-D-Ribitol Ligand Info
Structure Description Crystal structure of human orotidine-5'-monophosphate decarboxylase complexed with pyrazofurin monophosphate PDB:3MI2
Method X-ray diffraction Resolution 1.20 Å Mutation No [1]
PDB Sequence
KELSFGARAE
43
LPRIHPVASK
53
LLRLMQKKET
63
NLCLSADVSL
73
ARELLQLADA
83

LGPSICMLKT
93
HVDILNDFTL
103
DVMKELITLA
113
KHEFLIFEDR
124
KFADIGNTVK
134

KQYEGGIFKI
144
ASWADLVNAH
154
VVPGSGVVKG
164
LQEVGLPLHR
174
GCLLIAEMSS
184

TGSLATGDYT
194
RAAVRMAEEH
204
SEFVVGFISG
214
SRVSMKPEFL
224
HLTPGVQLEA
234

GGDNLGQQYN
244
SPQEVIGKRG
254
SDIIIVGRGI
264
ISAADRLEAA
274
EMYRKAAWEA
284

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .PFU or .PFU2 or .PFU3 or :3PFU;style chemicals stick;color identity;select .A:68 or .A:70 or .A:92 or .A:94 or .A:123 or .A:125 or .A:152 or .A:179 or .A:181 or .A:182 or .A:183 or .A:184 or .A:212 or .A:228 or .A:229 or .A:230 or .A:241 or .A:243 or .A:259 or .A:260 or .A:261 or .A:262 or .A:263; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.201
ASP70
2.740
LYS92
2.905
HIS94
2.928
ASP123
3.680
LYS125
2.605
ASN152
4.886
ILE179
4.038
GLU181
3.829
MET182
3.041
SER183
2.754
SER184
4.894
Residue
Distance (Å)
ILE212
3.483
PRO228
3.215
GLY229
4.536
VAL230
4.443
GLN241
2.879
TYR243
2.692
ILE259
4.007
VAL260
3.982
GLY261
2.880
ARG262
2.723
GLY263
4.814
Ligand Name: 2'-Deoxy-2'-Fluorouridine 5'-(Dihydrogen Phosphate) Ligand Info
Structure Description Crystal structure of human orotidine 5'-monophosphate decarboxylase covalently modified by 2'-fluoro-6-iodo-UMP PDB:3MO7
Method X-ray diffraction Resolution 1.35 Å Mutation No [9]
PDB Sequence
KELSFGARAE
43
LPRIHPVASK
53
LLRLMQKKET
63
NLCLSADVSL
73
ARELLQLADA
83

LGPSICMLKT
93
HVDILNDFTL
103
DVMKELITLA
113
KCHEFLIFED
123
RKFADIGNTV
133

KKQYEGGIFK
143
IASWADLVNA
153
HVVPGSGVVK
163
GLQEVGLPLH
173
RGCLLIAEMS
183

STGSLATGDY
193
TRAAVRMAEE
203
HSEFVVGFIS
213
GSRVSMKPEF
223
LHLTPGVQLE
233

AGGDNLGQQY
243
NSPQEVIGKR
253
GSDIIIVGRG
263
IISAADRLEA
273
AEMYRKAAWE
283

AYLSRLGV
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .UFT or .UFT2 or .UFT3 or :3UFT;style chemicals stick;color identity;select .A:68 or .A:70 or .A:92 or .A:94 or .A:123 or .A:125 or .A:181 or .A:182 or .A:183 or .A:212 or .A:228 or .A:229 or .A:230 or .A:241 or .A:243 or .A:259 or .A:260 or .A:261 or .A:262 or .A:263; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.189
ASP70
2.670
LYS92
2.979
HIS94
2.909
ASP123
3.468
LYS125
1.345
GLU181
4.145
MET182
3.216
SER183
2.803
ILE212
4.364
Residue
Distance (Å)
PRO228
3.371
GLY229
4.507
VAL230
4.419
GLN241
2.881
TYR243
2.702
ILE259
4.532
VAL260
3.989
GLY261
2.899
ARG262
2.793
GLY263
4.823
Ligand Name: 5-Cyano-Uridine-5'-Monophosphate Ligand Info
Structure Description Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Complexed with 5-CN-UMP PDB:3BK0
Method X-ray diffraction Resolution 1.60 Å Mutation No [10]
PDB Sequence
KELSFGARAE
43
LPRIHPVASK
53
LLRLMQKKET
63
NLCLSADVSL
73
ARELLQLADA
83

LGPSICMLKT
93
HVDILNDFTL
103
DVMKELITLA
113
KCHEFLIFED
123
RKFADIGNTV
133

KKQYEGGIFK
143
IASWADLVNA
153
HVVPGSGVVK
163
GLQEVGLPLH
173
RGCLLIAEMS
183

STGSLATGDY
193
TRAAVRMAEE
203
HSEFVVGFIS
213
GSRVSMKPEF
223
LHLTPGVQLE
233

AGGDNLGQQY
243
NSPQEVIGKR
253
GSDIIIVGRG
263
IISAADRLEA
273
AEMYRKAAWE
283

AYLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CNU or .CNU2 or .CNU3 or :3CNU;style chemicals stick;color identity;select .A:68 or .A:70 or .A:92 or .A:94 or .A:123 or .A:125 or .A:152 or .A:154 or .A:179 or .A:181 or .A:182 or .A:183 or .A:212 or .A:228 or .A:229 or .A:230 or .A:241 or .A:243 or .A:259 or .A:260 or .A:261 or .A:262 or .A:263; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER68
3.200
ASP70
2.699
LYS92
2.928
HIS94
3.281
ASP123
3.580
LYS125
4.298
ASN152
3.801
HIS154
4.857
ILE179
3.409
GLU181
4.307
MET182
3.242
SER183
2.777
Residue
Distance (Å)
ILE212
3.603
PRO228
3.286
GLY229
4.408
VAL230
4.504
GLN241
2.928
TYR243
2.745
ILE259
4.154
VAL260
3.936
GLY261
2.897
ARG262
2.797
GLY263
4.693
Ligand Name: N6-Acetyl-L-lysine Ligand Info
Structure Description OMPD-domain of human UMPS in complex with the substrate OMP at 0.99 Angstroms resolution PDB:7AM9
Method X-ray diffraction Resolution 0.99 Å Mutation No [4]
PDB Sequence
ELSFGARAEL
233
PRIHPVASKL
243
LRLMQKKETN
253
LCLSADVSLA
263
RELLQLADAL
273

GPSICMLKTH
283
VDILNDFTLD
293
VMKELITLAK
303
HEFLIFEDRF
315
ADIGNTVKKQ
325

YEGGIFKIAS
335
WADLVNAHVV
345
PGSGVVKGLQ
355
EVGLPLHRGC
365
LLIAEMSSTG
375

SLATGDYTRA
385
AVRMAEEHSE
395
FVVGFISGSR
405
VSMKPEFLHL
415
TPGVQLEAGG
425

DNLGQQYNSP
435
QEVIGKRGSD
445
IIIVGRGIIS
455
AADRLEAAEM
465
YRKAAWEAYL
475

SRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ALY or .ALY2 or .ALY3 or :3ALY;style chemicals stick;color identity;select .A:312 or .A:313 or .A:315 or .A:316 or .A:341 or .A:342 or .A:343 or .A:368 or .A:371 or .A:373; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP312
3.370
ARG313
1.334
PHE315
1.343
ALA316
3.300
ASN341
2.874
Residue
Distance (Å)
ALA342
4.364
HIS343
3.208
ILE368
3.582
MET371
3.196
SER373
4.329
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Orotidine-5'-monophosphate Ligand Info
Structure Description OMPD-domain of human UMPS in complex with the substrate OMP at 0.99 Angstroms resolution PDB:7AM9
Method X-ray diffraction Resolution 0.99 Å Mutation No [4]
PDB Sequence
ELSFGARAEL
233
PRIHPVASKL
243
LRLMQKKETN
253
LCLSADVSLA
263
RELLQLADAL
273

GPSICMLKTH
283
VDILNDFTLD
293
VMKELITLAK
303
HEFLIFEDRF
315
ADIGNTVKKQ
325

YEGGIFKIAS
335
WADLVNAHVV
345
PGSGVVKGLQ
355
EVGLPLHRGC
365
LLIAEMSSTG
375

SLATGDYTRA
385
AVRMAEEHSE
395
FVVGFISGSR
405
VSMKPEFLHL
415
TPGVQLEAGG
425

DNLGQQYNSP
435
QEVIGKRGSD
445
IIIVGRGIIS
455
AADRLEAAEM
465
YRKAAWEAYL
475

SRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OMP or .OMP2 or .OMP3 or :3OMP;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:310 or .A:312 or .A:341 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.211
ASP259
2.703
LYS281
2.911
HIS283
2.966
PHE310
4.697
ASP312
2.526
ASN341
3.359
GLU370
4.275
MET371
3.207
SER372
2.787
SER373
4.924
Residue
Distance (Å)
ILE401
3.822
PRO417
3.303
GLY418
4.417
VAL419
4.396
GLN430
2.927
TYR432
2.660
ILE448
3.892
VAL449
3.969
GLY450
2.877
ARG451
2.684
GLY452
4.740
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: [(2~{R},3~{S},4~{R},5~{R})-5-[6-carbamothioyl-2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate Ligand Info
Structure Description OMPD-domain of human UMPS in complex with 6-thiocarboxamido-UMP at 1.15 Angstroms resolution PDB:6ZX3
Method X-ray diffraction Resolution 1.15 Å Mutation No [4]
PDB Sequence
ELSFGARAEL
233
PRIHPVASKL
243
LRLMQKKETN
253
LCLSADVSLA
263
RELLQLADAL
273

GPSICMLKTH
283
VDILNDFTLD
293
VMKELITLAK
303
CHEFLIFEDR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .QRZ or .QRZ2 or .QRZ3 or :3QRZ;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:310 or .A:312 or .A:314 or .A:341 or .A:368 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.160
ASP259
2.746
LYS281
2.859
HIS283
3.351
PHE310
4.595
ASP312
2.857
LYS314
3.561
ASN341
3.875
ILE368
4.873
GLU370
4.247
MET371
3.089
SER372
2.774
Residue
Distance (Å)
SER373
4.819
ILE401
4.003
PRO417
3.397
GLY418
4.225
VAL419
4.400
GLN430
2.923
TYR432
2.663
ILE448
3.951
VAL449
3.961
GLY450
2.880
ARG451
2.727
GLY452
4.771
Ligand Name: [(2~{R},3~{S},4~{R},5~{R})-5-[6-aminocarbonyl-2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate Ligand Info
Structure Description OMPD-domain of human UMPS in complex with 6-carboxamido-UMP at 1.2 Angstroms resolution PDB:6ZX2
Method X-ray diffraction Resolution 1.20 Å Mutation No [4]
PDB Sequence
ELSFGARAEL
233
PRIHPVASKL
243
LRLMQKKETN
253
LCLSADVSLA
263
RELLQLADAL
273

GPSICMLKTH
283
VDILNDFTLD
293
VMKELITLAK
303
CHEFLIFEDR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .QRT or .QRT2 or .QRT3 or :3QRT;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:341 or .A:368 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.164
ASP259
2.724
LYS281
2.840
HIS283
3.243
ASP312
2.914
LYS314
3.716
ASN341
3.785
ILE368
4.731
GLU370
4.225
MET371
3.088
SER372
2.802
SER373
4.841
Residue
Distance (Å)
ILE401
3.974
PRO417
3.396
GLY418
4.225
VAL419
4.438
GLN430
2.934
TYR432
2.647
ILE448
4.024
VAL449
3.983
GLY450
2.885
ARG451
2.728
GLY452
4.744
Ligand Name: 5-Fluorouridine monophosphate Ligand Info
Structure Description Crystal structure of the orotidine-5'-monophosphate decarboxylase domain (Asp312Asn mutant) of human UMP synthase bound to 5-fluoro-UMP PDB:2QCF
Method X-ray diffraction Resolution 1.22 Å Mutation Yes [6]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KHEFLIFENR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .5FU or .5FU2 or .5FU3 or :35FU;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:341 or .A:368 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.146
ASP259
2.732
LYS281
2.857
HIS283
3.032
ASN312
3.505
LYS314
3.102
ASN341
4.838
ILE368
4.371
GLU370
4.206
MET371
3.138
SER372
2.726
SER373
4.998
Residue
Distance (Å)
ILE401
3.615
PRO417
3.304
GLY418
4.319
VAL419
4.377
GLN430
2.875
TYR432
2.659
ILE448
3.969
VAL449
3.937
GLY450
2.854
ARG451
2.720
GLY452
4.704
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 6-Acetyluridine 5'-phosphate Ligand Info
Structure Description Human orotidyl-5'-monophosphate decarboxylase in complex with 6-acetyl-UMP PDB:3L0K
Method X-ray diffraction Resolution 1.34 Å Mutation No [5]
PDB Sequence
MELSFGARAE
8
LPRIHPVASK
18
LLRLMQKKET
28
NLCLSADVSL
38
ARELLQLADA
48

LGPSICMLKT
58
HVDILNDFTL
68
DVMKELITLA
78
KCHEFLIFED
88
RKFADIGNTV
98

KKQYEGGIFK
108
IASWADLVNA
118
HVVPGSGVVK
128
GLQEVGLPLH
138
RGCLLIAEMS
148

STGSLATGDY
158
TRAAVRMAEE
168
HSEFVVGFIS
178
GSRVSMKPEF
188
LHLTPGVQLE
198

AGGDNLGQQY
208
NSPQEVIGKR
218
GSDIIIVGRG
228
IISAADRLEA
238
AEMYRKAAWE
248

AYLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6AU or .6AU2 or .6AU3 or :36AU;style chemicals stick;color identity;select .A:33 or .A:35 or .A:57 or .A:59 or .A:86 or .A:88 or .A:90 or .A:117 or .A:144 or .A:146 or .A:147 or .A:148 or .A:149 or .A:177 or .A:193 or .A:194 or .A:195 or .A:206 or .A:208 or .A:224 or .A:225 or .A:226 or .A:227 or .A:228; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER33
3.221
ASP35
2.746
LYS57
2.856
HIS59
2.914
PHE86
4.758
ASP88
3.350
LYS90
2.972
ASN117
3.230
ILE144
4.771
GLU146
4.323
MET147
3.137
SER148
2.798
Residue
Distance (Å)
SER149
4.775
ILE177
3.667
PRO193
3.394
GLY194
4.287
VAL195
4.479
GLN206
2.931
TYR208
2.676
ILE224
3.704
VAL225
3.995
GLY226
2.917
ARG227
2.739
GLY228
4.768
Ligand Name: 6-Cyanouridine 5'-Phosphate Ligand Info
Structure Description human orotidyl-5'-monophosphate decarboxylase in complex with 6-cyano-UMP PDB:3EX2
Method X-ray diffraction Resolution 1.55 Å Mutation No [5]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KCHEFLIFED
312
RKFADIGNTV
322

KKQYEGGIFK
332
IASWADLVNA
342
HVVPGSGVVK
352
GLQEVGLPLH
362
RGCLLIAEMS
372

STGSLATGDY
382
TRAAVRMAEE
392
HSEFVVGFIS
402
GSRVSMKPEF
412
LHLTPGVQLE
422

AGGDNLGQQY
432
NSPQEVIGKR
442
GSDIIIVGRG
452
IISAADRLEA
462
AEMYRKAAWE
472

AYLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6CN or .6CN2 or .6CN3 or :36CN;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:310 or .A:312 or .A:314 or .A:341 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.111
ASP259
2.614
LYS281
2.794
HIS283
3.036
PHE310
4.830
ASP312
3.432
LYS314
2.938
ASN341
4.582
GLU370
4.353
MET371
3.273
SER372
2.725
SER373
4.932
Residue
Distance (Å)
ILE401
4.260
PRO417
3.335
GLY418
4.235
VAL419
4.399
GLN430
2.716
TYR432
2.980
ILE448
3.947
VAL449
4.041
GLY450
3.012
ARG451
2.822
GLY452
4.804
Ligand Name: 6-Ethyluridine 5'-Phosphate Ligand Info
Structure Description D312N mutant of human orotidyl-5'-monophosphate decarboxylase in complex with 6-acetyl-UMP, covalent adduct PDB:3EWU
Method X-ray diffraction Resolution 1.60 Å Mutation Yes [5]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KCHEFLIFEN
312
RKFADIGNTV
322

KKQYEGGIFK
332
IASWADLVNA
342
HVVPGSGVVK
352
GLQEVGLPLH
362
RGCLLIAEMS
372

STGSLATGDY
382
TRAAVRMAEE
392
HSEFVVGFIS
402
GSRVSMKPEF
412
LHLTPGVQLE
422

AGGDNLGQQY
432
NSPQEVIGKR
442
GSDIIIVGRG
452
IISAADRLEA
462
AEMYRKAAWE
472

AYLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .UEP or .UEP2 or .UEP3 or :3UEP;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:310 or .A:312 or .A:314 or .A:341 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.291
ASP259
3.034
LYS281
2.861
HIS283
4.224
PHE310
4.648
ASN312
3.598
LYS314
1.364
ASN341
3.801
GLU370
4.228
MET371
3.112
SER372
2.809
SER373
4.828
Residue
Distance (Å)
ILE401
3.974
PRO417
3.380
GLY418
4.349
VAL419
4.411
GLN430
2.802
TYR432
2.705
ILE448
4.128
VAL449
3.879
GLY450
2.861
ARG451
2.825
GLY452
4.714
Ligand Name: 6-(Hydroxymethyl)uridine 5'-(Dihydrogen Phosphate) Ligand Info
Structure Description Crystal structure of the orotidine-5'-monophosphate decarboxylase domain (Asp312Asn mutant) of human UMP synthase bound to 6-hydroxymethyl-UMP PDB:2QCM
Method X-ray diffraction Resolution 1.67 Å Mutation Yes [6]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KHEFLIFENR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .JW5 or .JW52 or .JW53 or :3JW5;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:341 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.130
ASP259
2.766
LYS281
2.865
HIS283
3.157
ASN312
2.757
LYS314
4.211
ASN341
4.487
GLU370
4.189
MET371
3.129
SER372
2.742
SER373
4.888
Residue
Distance (Å)
ILE401
4.087
PRO417
3.353
GLY418
4.302
VAL419
4.383
GLN430
2.895
TYR432
2.669
ILE448
3.957
VAL449
3.968
GLY450
2.885
ARG451
2.742
GLY452
4.749
Ligand Name: 6-Sulfanyluridine-5'-phosphate Ligand Info
Structure Description Human orotidyl-5'-monophosphate decarboxylase in complex with 6-mercapto-UMP PDB:3L0N
Method X-ray diffraction Resolution 1.74 Å Mutation No [5]
PDB Sequence
ELSFGARAEL
9
PRIHPVASKL
19
LRLMQKKETN
29
LCLSADVSLA
39
RELLQLADAL
49

GPSICMLKTH
59
VDILNDFTLD
69
VMKELITLAK
79
CHEFLIFEDR
89
KFADIGNTVK
99

KQYEGGIFKI
109
ASWADLVNAH
119
VVPGSGVVKG
129
LQEVGLPLHR
139
GCLLIAEMSS
149

TGSLATGDYT
159
RAAVRMAEEH
169
SEFVVGFISG
179
SRVSMKPEFL
189
HLTPGVQLEA
199

GGDNLGQQYN
209
SPQEVIGKRG
219
SDIIIVGRGI
229
ISAADRLEAA
239
EMYRKAAWEA
249

YLSRL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S5P or .S5P2 or .S5P3 or :3S5P;style chemicals stick;color identity;select .A:33 or .A:35 or .A:57 or .A:59 or .A:88 or .A:90 or .A:117 or .A:146 or .A:147 or .A:148 or .A:149 or .A:177 or .A:193 or .A:194 or .A:195 or .A:206 or .A:208 or .A:224 or .A:225 or .A:226 or .A:227 or .A:228; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER33
3.230
ASP35
2.764
LYS57
2.868
HIS59
3.032
ASP88
3.318
LYS90
3.026
ASN117
4.490
GLU146
4.186
MET147
3.042
SER148
2.742
SER149
4.770
Residue
Distance (Å)
ILE177
3.825
PRO193
3.303
GLY194
4.676
VAL195
4.484
GLN206
2.959
TYR208
2.633
ILE224
3.732
VAL225
3.960
GLY226
2.907
ARG227
2.818
GLY228
4.775
Ligand Name: 5-Bromouridine 5'-monophosphate Ligand Info
Structure Description Crystal structure of the orotidine-5'-monophosphate decarboxylase domain of human UMP synthase bound to 5-bromo-UMP PDB:2QCG
Method X-ray diffraction Resolution 1.75 Å Mutation No [6]
PDB Sequence
AMELSFGARA
231
ELPRIHPVAS
241
KLLRLMQKKE
251
TNLCLSADVS
261
LARELLQLAD
271

ALGPSICMLK
281
THVDILNDFT
291
LDVMKELITL
301
AKCHEFLIFE
311
DRKFADIGNT
321

VKKQYEGGIF
331
KIASWADLVN
341
AHVVPGSGVV
351
KGLQEVGLPL
361
HRGCLLIAEM
371

SSTGSLATGD
381
YTRAAVRMAE
391
EHSEFVVGFI
401
SGSRVSMKPE
411
FLHLTPGVQL
421

EAGGDNLGQQ
431
YNSPQEVIGK
441
RGSDIIIVGR
451
GIISAADRLE
461
AAEMYRKAAW
471

EAYLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .5BU or .5BU2 or .5BU3 or :35BU;style chemicals stick;color identity;select .A:257 or .A:259 or .A:281 or .A:283 or .A:312 or .A:314 or .A:341 or .A:343 or .A:368 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.244
ASP259
2.929
LYS281
2.818
HIS283
3.053
ASP312
3.518
LYS314
4.206
ASN341
4.230
HIS343
4.905
ILE368
3.859
GLU370
4.326
MET371
3.268
SER372
2.761
Residue
Distance (Å)
SER373
4.873
ILE401
3.976
PRO417
3.343
GLY418
3.981
VAL419
4.470
GLN430
2.741
TYR432
2.924
ILE448
4.117
VAL449
4.001
GLY450
3.001
ARG451
2.843
GLY452
4.661
Ligand Name: Thiocysteine Ligand Info
Structure Description Human OMPD-domain of UMPS in complex with 6-hydroxy-UMP at 0.9 Angstroms resolution, crystal 1 PDB:7OUZ
Method X-ray diffraction Resolution 0.90 Å Mutation No [4]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KHEFLIFEDR
313
KFADIGNTVK
323

KQYEGGIFKI
333
ASWADLVNAH
343
VVPGSGVVKG
353
LQEVGLPLHR
363
GCLLIAEMSS
373

TGSLATGDYT
383
RAAVRMAEEH
393
SEFVVGFISG
403
SRVSMKPEFL
413
HLTPGVQLEA
423

GGDNLGQQYN
433
SPQEVIGKRG
443
SDIIIVGRGI
453
ISAADRLEAA
463
EMYRKAAWEA
473

YLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CSS or .CSS2 or .CSS3 or :3CSS;style chemicals stick;color identity;select .A:299 or .A:300 or .A:301 or .A:302 or .A:303 or .A:305 or .A:306; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE299
4.113
THR300
2.011
LEU301
2.561
ALA302
3.245
Residue
Distance (Å)
LYS303
1.329
HIS305
1.335
GLU306
2.990
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: 6-[(E)-iminomethyl]uridine 5'-phosphate Ligand Info
Structure Description D312N mutant of human orotidyl-5'-monophosphate decarboxylase in complex with 6-cyano-UMP, covalent adduct PDB:3EWW
Method X-ray diffraction Resolution 1.10 Å Mutation Yes [5]
PDB Sequence
MELSFGARAE
232
LPRIHPVASK
242
LLRLMQKKET
252
NLCLSADVSL
262
ARELLQLADA
272

LGPSICMLKT
282
HVDILNDFTL
292
DVMKELITLA
302
KCHEFLIFEN
312
RKFADIGNTV
322

KKQYEGGIFK
332
IASWADLVNA
342
HVVPGSGVVK
352
GLQEVGLPLH
362
RGCLLIAEMS
372

STGSLATGDY
382
TRAAVRMAEE
392
HSEFVVGFIS
402
GSRVSMKPEF
412
LHLTPGVQLE
422

AGGDNLGQQY
432
NSPQEVIGKR
442
GSDIIIVGRG
452
IISAADRLEA
462
AEMYRKAAWE
472

AYLSRLG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .U1P or .U1P2 or .U1P3 or :3U1P;style chemicals stick;color identity;select .A:257 or .A:281 or .A:283 or .A:310 or .A:312 or .A:314 or .A:341 or .A:370 or .A:371 or .A:372 or .A:373 or .A:401 or .A:417 or .A:418 or .A:419 or .A:430 or .A:432 or .A:448 or .A:449 or .A:450 or .A:451 or .A:452; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER257
3.152
LYS281
3.002
HIS283
2.924
PHE310
4.795
ASN312
3.551
LYS314
1.270
ASN341
3.656
GLU370
4.149
MET371
3.104
SER372
2.788
SER373
4.869
Residue
Distance (Å)
ILE401
3.972
PRO417
3.384
GLY418
4.255
VAL419
4.393
GLN430
2.934
TYR432
2.725
ILE448
4.118
VAL449
3.909
GLY450
2.849
ARG451
2.812
GLY452
4.698
References  Top
REF 1 Structural determinants for the inhibitory ligands of orotidine-5'-monophosphate decarboxylase. Bioorg Med Chem. 2010 Jun 1;18(11):4032-41.
REF 2 Structure-activity relationships of orotidine-5'-monophosphate decarboxylase inhibitors as anticancer agents. J Med Chem. 2009 Mar 26;52(6):1648-58.
REF 3 Crystal Structure of Human Orotidine 5'-Monophosphate Decarboxylase Complexed with 6-NH2-UMP
REF 4 Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5-monophosphate decarboxylase catalysis. doi:10.1038/s41929-022-00771-w.
REF 5 Lys314 is a nucleophile in non-classical reactions of orotidine-5'-monophosphate decarboxylase. Chemistry. 2009 Jul 6;15(27):6619-25.
REF 6 Structures of the human orotidine-5'-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug design. Structure. 2008 Jan;16(1):82-92.
REF 7 Novel cytidine-based orotidine-5'-monophosphate decarboxylase inhibitors with an unusual twist. J Med Chem. 2012 Nov 26;55(22):9988-97.
REF 8 Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Complexed with XMP
REF 9 Novel interactions of fluorinated nucleotide derivatives targeting orotidine 5'-monophosphate decarboxylase. J Med Chem. 2011 Apr 28;54(8):2891-901.
REF 10 Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Complexed with 5-CN-UMP

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