6FSH
Crystal structure of hybrid P450 OxyBtei(BC/FGvan)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0020037 | molecular_function | heme binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0020037 | molecular_function | heme binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue HEM A 401 |
| Chain | Residue |
| A | LEU88 |
| A | THR287 |
| A | ARG289 |
| A | LEU312 |
| A | ALA339 |
| A | PHE340 |
| A | GLY341 |
| A | HIS345 |
| A | CYS347 |
| A | GLY349 |
| A | THR353 |
| A | HIS96 |
| A | ARG100 |
| A | LEU152 |
| A | ALA236 |
| A | GLY237 |
| A | ASN240 |
| A | MET244 |
| A | PRO286 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | TYR284 |
| A | ARG383 |
| A | THR384 |
| A | SER385 |
| A | THR386 |
| A | ALA388 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue K A 403 |
| Chain | Residue |
| A | LEU235 |
| A | ASP238 |
| A | ASP239 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue HEM B 401 |
| Chain | Residue |
| B | LEU88 |
| B | MET89 |
| B | HIS96 |
| B | ARG100 |
| B | LEU152 |
| B | LEU155 |
| B | ALA236 |
| B | GLY237 |
| B | ASN240 |
| B | MET244 |
| B | PRO283 |
| B | PRO286 |
| B | THR287 |
| B | ARG289 |
| B | ALA339 |
| B | PHE340 |
| B | GLY341 |
| B | ILE344 |
| B | HIS345 |
| B | CYS347 |
| B | GLY349 |
| B | THR353 |
| B | HOH521 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| A | PRO376 |
| B | ARG100 |
| B | HIS346 |
| B | CYS347 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | binding site for residue HEM C 401 |
| Chain | Residue |
| C | LEU88 |
| C | MET89 |
| C | HIS96 |
| C | ARG100 |
| C | LEU152 |
| C | LEU155 |
| C | ALA236 |
| C | GLY237 |
| C | ASN240 |
| C | MET244 |
| C | PRO283 |
| C | PRO286 |
| C | THR287 |
| C | ARG289 |
| C | ALA339 |
| C | PHE340 |
| C | GLY341 |
| C | HIS345 |
| C | CYS347 |
| C | GLY349 |
| C | THR353 |
| C | HOH521 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | binding site for residue HEM D 401 |
| Chain | Residue |
| D | HOH519 |
| D | LEU88 |
| D | MET89 |
| D | HIS96 |
| D | ARG100 |
| D | LEU152 |
| D | LEU155 |
| D | ALA236 |
| D | GLY237 |
| D | ASN240 |
| D | VAL241 |
| D | MET244 |
| D | PRO283 |
| D | PRO286 |
| D | THR287 |
| D | ARG289 |
| D | ALA339 |
| D | PHE340 |
| D | GLY341 |
| D | HIS345 |
| D | CYS347 |
| D | GLY349 |
| D | THR353 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue ACT D 402 |
| Chain | Residue |
| C | PRO136 |
| D | HIS337 |
| D | HIS342 |
Functional Information from PROSITE/UniProt
