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2VCQ

Complex structure of prostaglandin D2 synthase at 1.95A.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001516biological_processprostaglandin biosynthetic process
A0004364molecular_functionglutathione transferase activity
A0004667molecular_functionprostaglandin-D synthase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006693biological_processprostaglandin metabolic process
A0007165biological_processsignal transduction
A0007626biological_processlocomotory behavior
A0009624biological_processresponse to nematode
A0010269biological_processresponse to selenium ion
A0016740molecular_functiontransferase activity
A0016853molecular_functionisomerase activity
A0042803molecular_functionprotein homodimerization activity
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
A2000255biological_processnegative regulation of male germ cell proliferation
B0000287molecular_functionmagnesium ion binding
B0001516biological_processprostaglandin biosynthetic process
B0004364molecular_functionglutathione transferase activity
B0004667molecular_functionprostaglandin-D synthase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006693biological_processprostaglandin metabolic process
B0007165biological_processsignal transduction
B0007626biological_processlocomotory behavior
B0009624biological_processresponse to nematode
B0010269biological_processresponse to selenium ion
B0016740molecular_functiontransferase activity
B0016853molecular_functionisomerase activity
B0042803molecular_functionprotein homodimerization activity
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
B2000255biological_processnegative regulation of male germ cell proliferation
C0000287molecular_functionmagnesium ion binding
C0001516biological_processprostaglandin biosynthetic process
C0004364molecular_functionglutathione transferase activity
C0004667molecular_functionprostaglandin-D synthase activity
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006693biological_processprostaglandin metabolic process
C0007165biological_processsignal transduction
C0007626biological_processlocomotory behavior
C0009624biological_processresponse to nematode
C0010269biological_processresponse to selenium ion
C0016740molecular_functiontransferase activity
C0016853molecular_functionisomerase activity
C0042803molecular_functionprotein homodimerization activity
C0043231cellular_componentintracellular membrane-bounded organelle
C0046872molecular_functionmetal ion binding
C2000255biological_processnegative regulation of male germ cell proliferation
D0000287molecular_functionmagnesium ion binding
D0001516biological_processprostaglandin biosynthetic process
D0004364molecular_functionglutathione transferase activity
D0004667molecular_functionprostaglandin-D synthase activity
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006693biological_processprostaglandin metabolic process
D0007165biological_processsignal transduction
D0007626biological_processlocomotory behavior
D0009624biological_processresponse to nematode
D0010269biological_processresponse to selenium ion
D0016740molecular_functiontransferase activity
D0016853molecular_functionisomerase activity
D0042803molecular_functionprotein homodimerization activity
D0043231cellular_componentintracellular membrane-bounded organelle
D0046872molecular_functionmetal ion binding
D2000255biological_processnegative regulation of male germ cell proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GSH A1200
ChainResidue
ATYR8
AHOH2032
BASP97
AARG14
ATRP39
ALYS43
ALYS50
AILE51
AGLN63
ASER64
AHOH2005

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GSH B1200
ChainResidue
AASP97
BTYR8
BARG14
BTRP39
BLYS43
BLYS50
BILE51
BGLN63
BSER64
BD251201
BHOH2059
BHOH2060
BHOH2103
BHOH2104
BHOH2105

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GSH C1200
ChainResidue
CTYR8
CARG14
CTRP39
CLYS43
CLYS50
CILE51
CPRO52
CGLN63
CSER64
CD251201
CHOH2023
CHOH2080
DASP97

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GSH D1200
ChainResidue
CASP97
DTYR8
DARG14
DTRP39
DLYS43
DLYS50
DILE51
DPRO52
DGLN63
DSER64
DHOH2081
DHOH2082
DHOH2083

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE D25 A1201
ChainResidue
AARG14
AMET99
ATYR152
AHOH2095

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE D25 B1201
ChainResidue
BMET11
BGLY13
BARG14
BMET99
BTRP104
BTYR152
BGSH1200
BHOH2101

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE D25 C1201
ChainResidue
CMET11
CGLY13
CARG14
CMET99
CTRP104
CTYR152
CLEU199
CGSH1200
CHOH2058

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518
ChainResidueDetails
ATYR8
BGLN63
CTYR8
CARG14
CTRP39
CGLY49
CGLN63
DTYR8
DARG14
DTRP39
DGLY49
AARG14
DGLN63
ATRP39
AGLY49
AGLN63
BTYR8
BARG14
BTRP39
BGLY49

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR8

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR8

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
CTYR8

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
DTYR8

229183

PDB entries from 2024-12-18

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