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3VI5

Human hematopoietic prostaglandin D synthase inhibitor complex structures

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
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
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
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
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 Residues12
DetailsBINDING SITE FOR RESIDUE GSH A 200
ChainResidue
ATYR8
ASER64
AHOH205
DASP697
AARG14
ATRP39
ALYS43
AGLY49
ALYS50
AILE51
APRO52
AGLN63

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GSH B 400
ChainResidue
BHOH78
BTYR208
BARG214
BTRP239
BLYS243
BLYS250
BILE251
BGLN263
BSER264
CASP497

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA C 901
ChainResidue
BHOH421
BHOH426
BHOH584
CASP496
CHOH619
CHOH644
CHOH690

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE M4M C 803
ChainResidue
CHOH68
CHOH84
CMET411
CGLY413
CARG414
CLYS450
CMET499
CTRP504
CTYR552
CHOH673
CHOH738

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 1001
ChainResidue
CGLN428
CTYR429
CHOH667
DHOH30
DHOH77
DTHR797

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 900
ChainResidue
AHOH470
AHOH640
DHOH278
DHOH509
DASP696

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE M4M D 804
ChainResidue
DHOH62
DGLY613
DARG614
DLYS650
DMET699
DTRP704
DTYR752
DHOH832
DHOH834

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
BGLN263
CTYR408
CARG414
CTRP439
CGLY449
CGLN463
DTYR608
DARG614
DTRP639
DGLY649
AARG14
DGLN663
ATRP39
AGLY49
AGLN63
BTYR208
BARG214
BTRP239
BGLY249

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PDB entries from 2024-07-17

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