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3B98

Crystal structure of zebrafish prostacyclin synthase (cytochrome P450 8A1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001516biological_processprostaglandin biosynthetic process
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0008116molecular_functionprostaglandin-I synthase activity
A0016020cellular_componentmembrane
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0106256molecular_functionhydroperoxy icosatetraenoate dehydratase activity
B0001516biological_processprostaglandin biosynthetic process
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0008116molecular_functionprostaglandin-I synthase activity
B0016020cellular_componentmembrane
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0106256molecular_functionhydroperoxy icosatetraenoate dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM A 600
ChainResidue
ALYS119
APHE426
AHOH642
AHOH663
AHOH768
AVAL273
ATHR274
AASN277
APRO413
ATRP414
ACYS421
APRO422
AGLY423

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM B 600
ChainResidue
BGLN94
BVAL273
BTHR274
BASN277
BALA278
BPRO413
BTRP414
BCYS421
BPRO422
BGLY423
BPHE426
BALA427
BILE465

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305|PubMed:18032380
ChainResidueDetails
AARG104
BARG362
ALEU110
AASN277
ATHR338
AARG362
BARG104
BLEU110
BASN277
BTHR338

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|PIRSR:PIRSR000047-1, ECO:0000269|PubMed:18032380, ECO:0007744|PDB:3B98, ECO:0007744|PDB:3B99
ChainResidueDetails
ACYS421
BCYS421

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PDB entries from 2024-11-06

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