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4EC0

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 Residues17
DetailsBINDING SITE FOR RESIDUE GSH A 201
ChainResidue
ATYR8
A7PQ203
AHOH301
AHOH402
AHOH464
AHOH472
AHOH652
AHOH684
BASP1097
AARG14
ATRP39
ALYS43
ALYS50
AILE51
APRO52
AGLN63
ASER64

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
AHOH412
AHOH423
AHOH459
BHOH1372
BHOH1384
BHOH1437

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 7PQ A 203
ChainResidue
ATYR8
AGLY13
AARG14
AASP96
AMET99
ATRP104
ATYR152
ATHR159
ALEU199
AGSH201
AHOH461

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GSH B 1201
ChainResidue
AASP97
BTYR1008
BARG1014
BTRP1039
BLYS1043
BLYS1050
BILE1051
BGLN1063
BSER1064
BHOH1309
BHOH1353
BHOH1404
BHOH1430
BHOH1438
BHOH1649

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
BGLN1063
AARG14
ATRP39
AGLY49
AGLN63
BTYR1008
BARG1014
BTRP1039
BGLY1049

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PDB entries from 2024-08-07

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