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5YWX

Crystal structure of hematopoietic prostaglandin D synthase in complex with F092

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 Residues14
Detailsbinding site for residue GSH A 301
ChainResidue
ATYR8
AHOH461
AHOH468
AHOH502
AHOH514
BASP97
AARG14
ATRP39
ALYS50
AILE51
APRO52
AGLN63
ASER64
A93C302

site_idAC2
Number of Residues14
Detailsbinding site for residue 93C A 302
ChainResidue
AMET11
AGLY13
AARG14
AGLN36
AMET99
ATRP104
AALA105
ATYR152
ALEU199
AGSH301
AHOH421
AHOH442
AHOH503
BGLY58

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL A 303
ChainResidue
AGLN196
ATHR197
AHOH415
AHOH444
AHOH505
AHOH542
DGLN28
DTYR29
DGOL303

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 304
ChainResidue
AGLN28
ATYR29
AHOH428
AHOH520
DGLN196
DTHR197
DLYS198

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 201
ChainResidue
AHOH456
AHOH488
AHOH529
BHOH304
BHOH322
BHOH329

site_idAC6
Number of Residues13
Detailsbinding site for residue GSH B 202
ChainResidue
AASP97
BTYR8
BARG14
BTRP39
BLYS43
BGLY49
BLYS50
BILE51
BPRO52
BGLN63
BSER64
BHOH328
BHOH350

site_idAC7
Number of Residues8
Detailsbinding site for residue 93C B 203
ChainResidue
BGLY13
BARG14
BGLN36
BMET99
BTRP104
BALA105
BTYR152
BHOH321

site_idAC8
Number of Residues6
Detailsbinding site for residue MG C 201
ChainResidue
CHOH322
CHOH329
CHOH334
DHOH452
DHOH483
DHOH485

site_idAC9
Number of Residues13
Detailsbinding site for residue GSH C 202
ChainResidue
CTYR8
CARG14
CTRP39
CLYS43
CLYS50
CILE51
CPRO52
CGLN63
CSER64
C93C203
CHOH325
CHOH336
DASP97

site_idAD1
Number of Residues11
Detailsbinding site for residue 93C C 203
ChainResidue
CGSH202
CHOH310
CMET11
CGLY13
CARG14
CGLN36
CMET99
CTRP104
CALA105
CTYR152
CLEU199

site_idAD2
Number of Residues12
Detailsbinding site for residue GSH D 301
ChainResidue
CASP97
DTYR8
DARG14
DTRP39
DLYS50
DILE51
DPRO52
DGLN63
DSER64
D93C302
DHOH430
DHOH459

site_idAD3
Number of Residues13
Detailsbinding site for residue 93C D 302
ChainResidue
CLEU59
DMET11
DGLY13
DARG14
DGLN36
DMET99
DTRP104
DALA105
DTYR152
DLEU199
DGSH301
DHOH416
DHOH446

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL D 303
ChainResidue
ALYS198
AGOL303
DGLN28
DTYR29
DHOH415
DHOH436
DHOH540

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

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PDB entries from 2024-07-17

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