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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
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0007165biological_processsignal transduction
A0007626biological_processlocomotory behavior
A0016740molecular_functiontransferase activity
A0016853molecular_functionisomerase activity
A0019371biological_processcyclooxygenase pathway
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0001516biological_processprostaglandin biosynthetic process
B0004364molecular_functionglutathione transferase activity
B0004667molecular_functionprostaglandin-D synthase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006693biological_processprostaglandin metabolic process
B0006749biological_processglutathione metabolic process
B0007165biological_processsignal transduction
B0007626biological_processlocomotory behavior
B0016740molecular_functiontransferase activity
B0016853molecular_functionisomerase activity
B0019371biological_processcyclooxygenase pathway
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
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 Residues154
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues118
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12627223","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15113825","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16547010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18341273","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19939518","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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