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6ZTC

CRYSTAL STRUCTURE OF PROSTAGLANDIN D2 SYNTHASE IN COMPLEX WITH FRAGMENT 1A AT 1.84A RESOLUTION.

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
AHOH324
AHOH340
AHOH374
AHOH386
AHOH421
AHOH424
AHOH450
BASP97
AARG14
ATRP39
ALYS43
ALYS50
AILE51
AGLN63
ASER64
AQPN203

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 202
ChainResidue
AHOH351
AHOH385
AHOH442
BHOH340
BHOH352
BHOH392

site_idAC3
Number of Residues10
Detailsbinding site for residue QPN A 203
ChainResidue
AGLY13
AARG14
AASP96
AMET99
ASER100
ATRP104
ATYR152
ALEU199
AGSH201
AHOH355

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 204
ChainResidue
AGLU82
AHOH359
BTYR70
BLYS73

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 205
ChainResidue
AGLU55
ATHR60
AHOH481

site_idAC6
Number of Residues16
Detailsbinding site for residue GSH B 201
ChainResidue
AASP97
BTYR8
BARG14
BTRP39
BLYS43
BLYS50
BILE51
BGLN63
BSER64
BQPN202
BHOH328
BHOH346
BHOH397
BHOH404
BHOH449
BHOH502

site_idAC7
Number of Residues13
Detailsbinding site for residue QPN B 202
ChainResidue
BTYR8
BMET11
BGLY13
BARG14
BASP96
BMET99
BSER100
BTRP104
BTYR152
BTHR159
BLEU199
BGSH201
BHOH332

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 203
ChainResidue
BLYS112
BHOH307
BHOH316
BHOH487

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 2024-07-24

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