Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2QCC

Crystal structure of the orotidine-5'-monophosphate decarboxylase domain of human UMP synthase, apo form

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
B0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 481
ChainResidue
ATYR432
AGLY450
AARG451
AGOL482
AHOH562
AHOH597

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 481
ChainResidue
BGOL482
BHOH512
BHOH519
BHOH584
BHOH600
BTYR432
BGLY450
BARG451

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 482
ChainResidue
ASER257
AASP259
ALYS281
AHIS283
AILE448
ASO4481
BASP317
BTHR321

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 482
ChainResidue
AASP317
ATHR321
AHOH630
BSER257
BASP259
BLYS281
BHIS283
BASP312
BSO4481

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 Residues6
DetailsActive site: {"description":"For OMPdecase activity","evidences":[{"source":"PubMed","id":"18184586","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18184586","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QCD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
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 Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18184586","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QCL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
BLYS314
BASP312

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
ALYS281
AASP317
ALYS314
AASP312

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dbt
ChainResidueDetails
BLYS281
BASP317
BLYS314
BASP312

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon