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3G3D

Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified by 5-fluoro-6-azido-UMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0044205biological_process'de novo' UMP biosynthetic process
B0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5FU A3000
ChainResidue
ASER68
AGLN241
ATYR243
AGLY261
AARG262
AHOH295
AHOH297
AHOH298
AHOH330
BASP128
BILE129
AASP70
BTHR132
ALYS92
AHIS94
AASP123
ALYS125
AMET182
ASER183
APRO228

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 5FU B3000
ChainResidue
AASP128
AILE129
ATHR132
BSER68
BASP70
BLYS92
BHIS94
BASP123
BLYS125
BMET182
BSER183
BPRO228
BGLN241
BTYR243
BGLY261
BARG262
BHOH300
BHOH338
BHOH345

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1000
ChainResidue
ALYS53
AALA113
ALYS114
APHE118
ALEU119
AASP149
AHOH390

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B1001
ChainResidue
BLEU73
BARG75

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B1002
ChainResidue
BASP269
BGLU272
BMET276
BHOH348
BHOH425

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B2000
ChainResidue
BGLY39
BALA40
BGLU43
BHOH359

Functional Information from PROSITE/UniProt
site_idPS00156
Number of Residues14
DetailsOMPDECASE Orotidine 5'-phosphate decarboxylase active site. IFeDrKfaDIGnTV
ChainResidueDetails
AILE120-VAL133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: For OMPdecase activity => ECO:0000269|PubMed:18184586
ChainResidueDetails
AASP123
ALYS125
AASP128
BASP123
BLYS125
BASP128

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD
ChainResidueDetails
ATHR132
BSER68
BASP128
BTHR132
ASER68
AASP128

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
ChainResidueDetails
AASP70
ASER183
BASP70
BSER183
BGLN241
BGLY261
AGLN241
AGLY261

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCL
ChainResidueDetails
ALYS92
ALYS125
BLYS92
BLYS125

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER25
BSER25

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PDB entries from 2024-06-12

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