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3MO7

Crystal structure of human orotidine 5'-monophosphate decarboxylase covalently modified by 2'-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 UFT A 3000
ChainResidue
AHOH3
AASP128
AILE129
ATHR132
AMET182
ASER183
APRO228
AGLN241
ATYR243
AGLY261
AARG262
AHOH4
AHOH295
AHOH5
ASER68
AASP70
ALYS92
AHIS94
AASP123
ALYS125

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1000
ChainResidue
ALYS53
AALA113
APHE118
ALEU119
AASP149
AHOH359
AHOH402

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
DetailsActive site: {"description":"For OMPdecase activity","evidences":[{"source":"PubMed","id":"18184586","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18184586","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QCD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18184586","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QCD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QCH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18184586","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QCL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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