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6ZX3

OMPD-domain of human UMPS in complex with 6-thiocarboxamido-UMP at 1.15 Angstroms resolution

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 Residues19
Detailsbinding site for residue QRZ A 501
ChainResidue
ASER257
AMET371
ASER372
APRO417
AGLN430
ATYR432
AGLY450
AARG451
AHOH630
AHOH633
AHOH661
AASP259
ALYS281
AHIS283
AASP312
ALYS314
AASP317
AILE318
ATHR321

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 502
ChainResidue
ATHR374
AGLY429
AHOH609
AHOH698

site_idAC3
Number of Residues8
Detailsbinding site for residue PRO A 503
ChainResidue
AGLY228
AGLU232
ALEU421
AHOH606
AHOH749
AHOH858
AHOH879
AHOH926

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 504
ChainResidue
ASER348
ALYS352
AHIS393
AHOH669
AHOH690

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 Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD
ChainResidueDetails
APRO435

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
ChainResidueDetails
AGLU437

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCL
ChainResidueDetails
AARG459

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
AGLU392

223532

PDB entries from 2024-08-07

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