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3G3M

Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified by 5-fluoro-6-iodo-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
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5FU A 1000
ChainResidue
AHOH2
ALYS125
AASP128
AILE129
ATHR132
AMET182
ASER183
APRO228
AGLN241
ATYR243
AGLY261
AHOH3
AARG262
AHOH5
AHOH9
ASER68
AASP70
ALYS92
AHIS94
AASP123

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 Residues3
DetailsACT_SITE: For OMPdecase activity => ECO:0000269|PubMed:18184586
ChainResidueDetails
AASP123
ALYS125
AASP128

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD
ChainResidueDetails
ASER68
AASP128
ATHR132

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
ChainResidueDetails
AASP70
ASER183
AGLN241
AGLY261

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCL
ChainResidueDetails
ALYS92
ALYS125

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

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
ALYS92
AASP123
ALYS125
AASP128

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PDB entries from 2024-10-09

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