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4EDY

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 201
ChainResidue
AHOH3312
AHOH3313
AHOH3314
BHOH667
BHOH668
BHOH669

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GSH A 202
ChainResidue
ALYS43
ALYS50
AILE51
APRO52
AGLN63
ASER64
A9PQ203
AHOH3002
AHOH3104
AHOH3167
AHOH3169
AHOH3177
AHOH3195
AHOH3262
AHOH3278
BASP97
ATYR8
AARG14
ATRP39

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 9PQ A 203
ChainResidue
ATYR8
AGLY13
AARG14
AGLN36
AASP96
AMET99
ATRP104
ATYR152
ATHR159
ALEU199
AGSH202
AHOH3164
AHOH3278

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS B 201
ChainResidue
BGLY13
BMET99
BTYR152

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GSH B 202
ChainResidue
AASP97
BTYR8
BARG14
BTRP39
BLYS43
BLYS50
BILE51
BGLN63
BSER64
BHOH309
BHOH352
BHOH399
BHOH430
BHOH437
BHOH493
BHOH628
BHOH645

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
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
AARG14
ATRP39
AGLY49
AGLN63
BTYR8
BARG14
BTRP39
BGLY49

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PDB entries from 2024-07-10

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