1IZO
Cytochrome P450 BS beta Complexed with Fatty Acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006696 | biological_process | ergosterol biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase 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 | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006696 | biological_process | ergosterol biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase 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 | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0006696 | biological_process | ergosterol biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | TYR59 |
| A | ALA246 |
| A | ILE247 |
| A | PHE250 |
| A | PHE289 |
| A | LEU293 |
| A | GLN352 |
| A | HIS361 |
| A | CYS363 |
| A | PRO364 |
| A | ILE368 |
| A | ARG66 |
| A | THR369 |
| A | HOH627 |
| A | HOH631 |
| A | ILE84 |
| A | HIS92 |
| A | LYS96 |
| A | PHE99 |
| A | MET103 |
| A | VAL240 |
| A | PRO243 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | TYR59 |
| B | ARG66 |
| B | ILE84 |
| B | HIS92 |
| B | LYS96 |
| B | PHE99 |
| B | MET103 |
| B | VAL240 |
| B | PRO243 |
| B | ILE244 |
| B | ALA246 |
| B | ILE247 |
| B | PHE250 |
| B | PHE289 |
| B | LEU293 |
| B | LEU318 |
| B | GLN352 |
| B | HIS361 |
| B | CYS363 |
| B | PRO364 |
| B | GLY365 |
| B | HOH1639 |
| B | HOH1677 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | TYR59 |
| C | ARG66 |
| C | ILE84 |
| C | HIS92 |
| C | LYS96 |
| C | MET103 |
| C | PRO243 |
| C | ILE244 |
| C | ILE247 |
| C | PHE250 |
| C | PHE289 |
| C | LEU293 |
| C | GLN352 |
| C | GLY360 |
| C | HIS361 |
| C | ARG362 |
| C | CYS363 |
| C | PRO364 |
| C | ILE368 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PAM A 601 |
| Chain | Residue |
| A | VAL170 |
| A | ARG242 |
| A | PHE289 |
| A | PHE292 |
| B | LEU205 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PAM B 1601 |
| Chain | Residue |
| B | PHE173 |
| B | ARG242 |
| B | PRO243 |
| B | PHE292 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PAM C 2601 |
| Chain | Residue |
| C | LEU42 |
| C | VAL170 |
| C | ARG242 |
| C | PHE292 |
| C | HOH2650 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:12519760 |
| Chain | Residue | Details |
| A | CYS363 | |
| B | CYS363 | |
| C | CYS363 |
