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3EX4

human orotidyl-5'-monophosphate decarboxylase in complex with BMP

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 Residues21
DetailsBINDING SITE FOR RESIDUE BMP A 481
ChainResidue
ASER257
AMET371
ASER372
APRO417
AGLN430
ATYR432
AGLY450
AARG451
AHOH483
AHOH484
AHOH494
AASP259
AHOH498
AHOH517
ALYS281
AHIS283
AASP312
ALYS314
AASP317
AILE318
ATHR321

Functional Information from PROSITE/UniProt
site_idPS00156
Number of Residues14
DetailsOMPDECASE Orotidine 5'-phosphate decarboxylase active site. IFeDrKfaDIGnTV
ChainResidueDetails
AILE309-VAL322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: For OMPdecase activity => ECO:0000269|PubMed:18184586
ChainResidueDetails
AASP312
ALYS314
AASP317

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD
ChainResidueDetails
ASER257
AASP317
ATHR321

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
ChainResidueDetails
AASP259
ASER372
AGLN430
AGLY450

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCL
ChainResidueDetails
ALYS281
ALYS314

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
ALYS314
AASP312

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
ALYS281
AASP317
ALYS314
AASP312

221716

PDB entries from 2024-06-26

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