3B99
Crystal structure of zebrafish prostacyclin synthase (cytochrome P450 8A1) in complex with substrate analog U51605
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 | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 600 |
| Chain | Residue |
| A | GLN94 |
| A | TRP414 |
| A | GLY415 |
| A | ASN419 |
| A | CYS421 |
| A | PRO422 |
| A | GLY423 |
| A | ILE465 |
| A | U51700 |
| A | HOH704 |
| A | LYS119 |
| A | PHE126 |
| A | VAL273 |
| A | THR274 |
| A | ASN277 |
| A | ALA335 |
| A | ARG339 |
| A | PRO413 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE U51 A 700 |
| Chain | Residue |
| A | VAL273 |
| A | ASN277 |
| A | ALA335 |
| A | LEU336 |
| A | ILE337 |
| A | THR338 |
| A | ARG339 |
| A | GLY462 |
| A | HEM600 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE U51 A 701 |
| Chain | Residue |
| A | ALA98 |
| A | GLN99 |
| A | MET102 |
| A | ILE105 |
| A | PHE106 |
| A | LEU110 |
| A | HIS113 |
| A | TRP272 |
| A | HOH732 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE U51 A 702 |
| Chain | Residue |
| A | PHE45 |
| A | TYR97 |
| A | ARG104 |
| A | ARG362 |
| A | CYS364 |
| A | GLY462 |
| A | PHE463 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM B 600 |
| Chain | Residue |
| B | GLN94 |
| B | LYS119 |
| B | PHE126 |
| B | VAL273 |
| B | THR274 |
| B | ASN277 |
| B | ARG339 |
| B | PRO413 |
| B | TRP414 |
| B | ASN419 |
| B | CYS421 |
| B | PRO422 |
| B | GLY423 |
| B | ILE465 |
| B | U51700 |
| B | HOH738 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE U51 B 700 |
| Chain | Residue |
| B | GLN94 |
| B | ALA98 |
| B | VAL273 |
| B | ASN277 |
| B | ALA335 |
| B | LEU336 |
| B | ILE337 |
| B | THR338 |
| B | ARG339 |
| B | GLY462 |
| B | HEM600 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE U51 B 701 |
| Chain | Residue |
| B | GLU118 |
| B | ALA122 |
| B | TRP245 |
| B | TYR249 |
| B | LEU269 |
| B | GLN270 |
| B | TRP272 |
| B | U51702 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE U51 B 702 |
| Chain | Residue |
| B | ILE73 |
| B | TYR97 |
| B | ARG209 |
| B | LEU336 |
| B | ARG362 |
| B | GLY462 |
| B | PHE463 |
| B | U51701 |
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 |
| 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 |
