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

6ZX2

OMPD-domain of human UMPS in complex with 6-carboxamido-UMP at 1.2 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 Residues18
Detailsbinding site for residue QRT A 501
ChainResidue
ASER257
ASER372
APRO417
AGLN430
ATYR432
AGLY450
AARG451
AHOH631
AHOH652
AHOH657
AASP259
ALYS281
AHIS283
AASP312
AASP317
AILE318
ATHR321
AMET371

site_idAC2
Number of Residues8
Detailsbinding site for residue PRO A 502
ChainResidue
AGLY228
AALA229
AGLU232
ALEU421
AHOH671
AHOH853
AHOH878
AHOH933

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 503
ChainResidue
ASER348
ALYS352
AHIS393
AHOH655
AHOH910
AHOH945

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon