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 | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0008116 | molecular_function | prostaglandin-I synthase activity |
A | 0016020 | cellular_component | membrane |
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 | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0008116 | molecular_function | prostaglandin-I synthase activity |
B | 0016020 | cellular_component | membrane |
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: BINDING => ECO:0000305|PubMed:18032380 |
Chain | Residue | Details |
A | ARG104 | |
B | ARG362 | |
A | LEU110 | |
A | ASN277 | |
A | THR338 | |
A | ARG362 | |
B | ARG104 | |
B | LEU110 | |
B | ASN277 | |
B | THR338 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000255|PIRSR:PIRSR000047-1, ECO:0000269|PubMed:18032380, ECO:0007744|PDB:3B98, ECO:0007744|PDB:3B99 |
Chain | Residue | Details |
A | CYS421 | |
B | CYS421 |