Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3BVJ

Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Complexed with XMP

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 Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 4000
ChainResidue
ASER159
ALYS163
AHIS204

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 4001
ChainResidue
BSER159
BLYS163
BHIS204

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE XMP A 2000
ChainResidue
AHIS94
ALYS125
AASN152
AMET182
ASER183
AILE212
APRO228
AGLN241
ATYR243
AGLY261
AARG262
BASP128
BILE129
BTHR132
ASER68
AASP70
ALYS92

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE XMP B 2000
ChainResidue
AASP128
AILE129
ATHR132
BSER68
BASP70
BLYS92
BHIS94
BLYS125
BASN152
BMET182
BSER183
BILE212
BPRO228
BGLN241
BTYR243
BGLY261
BARG262

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 3000
ChainResidue
AARG46
ASER205

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
ASER68
AASP128
ATHR132
BSER68
BASP128
BTHR132

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

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
AASP123
ALYS125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
BASP123
BLYS125

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
ALYS92
AASP123
ALYS125
AASP128

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
BLYS92
BASP123
BLYS125
BASP128

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon