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

3EWY

K314A mutant of human orotidyl-5'-monophosphate decarboxylase soaked with OMP, decarboxylated to 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 Residues18
DetailsBINDING SITE FOR RESIDUE U5P A 481
ChainResidue
ASER257
ASER372
APRO417
AGLN430
ATYR432
AGLY450
AARG451
AHOH484
AHOH487
AHOH494
AASP259
ALYS281
AHIS283
AASP312
AASP317
AILE318
ATHR321
AMET371

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 482
ChainResidue
AGLY228
AALA229
AGLU232
AGLN248
ALEU421
AGLU422
AALA423
AHOH540
AHOH597

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 483
ChainResidue
ALYS242
AILE299
AALA302
ALYS303
APHE307
ALEU308
AASP338
AHOH592
AHOH603
AHOH761
AHOH811

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: For OMPdecase activity => ECO:0000269|PubMed:18184586
ChainResidueDetails
AASP312
AALA314
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
AALA314

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
AALA314
AASP312

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon