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4EE0

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
AHOH318
AHOH323
AHOH334
BHOH317
BHOH349
BHOH356

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 0O4 A 202
ChainResidue
AASP96
AMET99
ATRP104
ATYR152
ALEU199
AGSF203
AHOH320
AMET11
AGLY13
AARG14

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GSF A 203
ChainResidue
ATYR8
APHE9
AARG14
ALYS43
AGLY49
ALYS50
AILE51
APRO52
AGLN63
ASER64
A0O4202
AHOH326
AHOH327
AHOH355
AHOH357
AHOH398
BASP97

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 0O4 B 201
ChainResidue
BPHE9
BMET11
BGLY13
BARG14
BASP96
BMET99
BSER100
BTRP104
BTYR152
BGSF202
BHOH344
BHOH430
BHOH453

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GSF B 202
ChainResidue
AASP97
BTYR8
BPHE9
BARG14
BTRP39
BLYS43
BLYS50
BILE51
BGLN63
BSER64
B0O4201
BHOH318
BHOH321
BHOH322
BHOH325
BHOH427

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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