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4EDZ

Crystal structure of hH-PGDS with water displacing inhibitor

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 Residues16
DetailsBINDING SITE FOR RESIDUE GSH A 201
ChainResidue
ATYR8
AHOH303
AHOH304
AHOH321
AHOH360
AHOH405
AHOH414
BASP97
AARG14
ATRP39
ALYS43
ALYS50
AILE51
APRO52
AGLN63
ASER64

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0O5 A 202
ChainResidue
AMET11
AGLY13
AARG14
AGLN36
AASP96
AMET99
ATRP104
ATYR152
AILE155
ALEU199
AHOH319
AHOH378

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 201
ChainResidue
AHOH301
AHOH302
BHOH301
BHOH302

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GSH B 202
ChainResidue
AASP97
BTYR8
BARG14
BTRP39
BLYS43
BLYS50
BILE51
BPRO52
BGLN63
BSER64
B0O5203
BHOH308
BHOH312
BHOH353
BHOH371

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 0O5 B 203
ChainResidue
BPHE9
BMET11
BGLY13
BARG14
BGLN36
BASP96
BMET99
BSER100
BTRP104
BTYR152
BILE155
BLEU199
BGSH202
BHOH321

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 201
ChainResidue
CHOH301
CHOH302
CHOH303
DHOH2501
DHOH2502
DHOH2503

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GSH C 202
ChainResidue
CTYR8
CARG14
CTRP39
CLYS43
CLYS50
CILE51
CGLN63
CSER64
CHOH332
CHOH340
CHOH351
DASP97

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0O5 C 203
ChainResidue
CGLY13
CARG14
CGLN36
CASP96
CMET99
CSER100
CTRP104
CTYR152
CILE155
CLEU199
CHOH346
CHOH391

site_idAC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GSH D 201
ChainResidue
DSER64
D0O5202
DHOH2504
DHOH2505
DHOH2523
DHOH2544
DHOH2586
DHOH2616
CASP97
DTYR8
DARG14
DTRP39
DLYS43
DLYS50
DILE51
DGLN63

site_idBC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 0O5 D 202
ChainResidue
DTYR8
DPHE9
DMET11
DGLY13
DARG14
DGLN36
DASP96
DMET99
DTRP104
DTYR152
DILE155
DGSH201
DHOH2520
DHOH2592

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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