3B98

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001516	biological_process	prostaglandin biosynthetic process
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006693	biological_process	prostaglandin metabolic process
A	0008116	molecular_function	prostaglandin-I synthase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0106256	molecular_function	hydroperoxy icosatetraenoate dehydratase activity
B	0001516	biological_process	prostaglandin biosynthetic process
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006693	biological_process	prostaglandin metabolic process
B	0008116	molecular_function	prostaglandin-I synthase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0106256	molecular_function	hydroperoxy icosatetraenoate dehydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM A 600

Chain	Residue
A	LYS119
A	PHE426
A	HOH642
A	HOH663
A	HOH768
A	VAL273
A	THR274
A	ASN277
A	PRO413
A	TRP414
A	CYS421
A	PRO422
A	GLY423

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM B 600

Chain	Residue
B	GLN94
B	VAL273
B	THR274
B	ASN277
B	ALA278
B	PRO413
B	TRP414
B	CYS421
B	PRO422
B	GLY423
B	PHE426
B	ALA427
B	ILE465

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18032380","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PIRSR","id":"PIRSR000047-1","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18032380","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3B98","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B99","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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