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 | 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 | 0020037 | molecular_function | heme 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 | 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 | 0020037 | molecular_function | heme 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 |
| 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 |
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 |
