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1IYI

Crystal structure of hematopoietic prostaglandin D synthase

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 Residues7
DetailsBINDING SITE FOR RESIDUE CA D 1900
ChainResidue
AHOH1259
AHOH1284
AHOH1437
DASP696
DHOH1908
DHOH2009
DHOH2030

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA C 1901
ChainResidue
BHOH1473
CASP496
CHOH1988
CHOH1989
CHOH2004
BHOH1432
BHOH1433

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GSH A 1200
ChainResidue
ATYR8
AARG14
ATRP39
ALYS50
AILE51
AGLN63
ASER64
AHOH1224
AHOH1225
AHOH1229
AHOH1254
AHOH1257
AHOH1419
AHOH1422
DASP697

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GSH B 1400
ChainResidue
BTYR208
BARG214
BTRP239
BLYS243
BLYS250
BILE251
BGLN263
BSER264
BHOH1427
BHOH1431
BHOH1458
BHOH1461
BHOH1510
BHOH1517
CASP497

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GSH C 1600
ChainResidue
BASP297
CTYR408
CARG414
CTRP439
CLYS443
CLYS450
CILE451
CPRO452
CGLN463
CSER464
CHOH1925
CHOH1928
CHOH2005
CHOH2035
CHOH2052
CHOH2070

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GSH D 1800
ChainResidue
AASP97
DTYR608
DARG614
DTRP639
DLYS643
DLYS650
DILE651
DGLN663
DSER664
DHOH1910
DHOH1960
DHOH2015
DHOH2017
DHOH2043
DHOH2068
DHOH2119

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
APHE9
BSER264
CPHE409
CALA415
CPRO440
CLYS450
CSER464
DPHE609
DALA615
DPRO640
DLYS650
AALA15
DSER664
APRO40
ALYS50
ASER64
BPHE209
BALA215
BPRO240
BLYS250

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
BTYR208

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
CTYR408

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
DTYR608

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PDB entries from 2024-10-30

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