3MGX
Crystal Structure of P450 OxyD that is involved in the Biosynthesis of Vancomycin-type Antibiotics
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006707 | biological_process | cholesterol catabolic process |
| B | 0008395 | molecular_function | steroid hydroxylase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| B | 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 397 |
| Chain | Residue |
| A | MET70 |
| A | LEU276 |
| A | VAL285 |
| A | ARG287 |
| A | THR337 |
| A | PHE338 |
| A | GLY339 |
| A | HIS343 |
| A | CYS345 |
| A | GLY347 |
| A | GOL399 |
| A | MET87 |
| A | HOH432 |
| A | HOH448 |
| A | HOH459 |
| A | VAL88 |
| A | HIS95 |
| A | ARG99 |
| A | GLY235 |
| A | GLY236 |
| A | THR239 |
| A | THR240 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 398 |
| Chain | Residue |
| A | GLU19 |
| A | HOH439 |
| A | HOH468 |
| A | HOH469 |
| B | LEU18 |
| B | HIS21 |
| B | HIS249 |
| B | TRP278 |
| B | ARG315 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 399 |
| Chain | Residue |
| A | MET70 |
| A | ASN231 |
| A | GLY235 |
| A | HEM397 |
| A | GOL400 |
| A | HOH448 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 400 |
| Chain | Residue |
| A | MET70 |
| A | MET71 |
| A | ASP80 |
| A | VAL88 |
| A | GOL399 |
| A | HOH460 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 401 |
| Chain | Residue |
| A | LEU18 |
| A | HIS249 |
| A | TRP278 |
| A | ARG315 |
| A | TRP377 |
| B | GLU19 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | ARG99 |
| A | HIS344 |
| A | CYS345 |
| A | LEU346 |
| A | SER348 |
| A | HOH416 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM B 397 |
| Chain | Residue |
| B | MET70 |
| B | MET87 |
| B | VAL88 |
| B | HIS95 |
| B | ARG99 |
| B | GLY235 |
| B | GLY236 |
| B | THR239 |
| B | THR240 |
| B | LEU276 |
| B | VAL285 |
| B | ARG287 |
| B | THR337 |
| B | PHE338 |
| B | GLY339 |
| B | HIS343 |
| B | CYS345 |
| B | GLY347 |
| B | GOL399 |
| B | HOH440 |
| B | HOH448 |
| B | HOH498 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 398 |
| Chain | Residue |
| B | MET71 |
| B | ASP80 |
| B | ILE234 |
| B | GOL399 |
| B | HOH406 |
| B | HOH429 |
| B | HOH506 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 399 |
| Chain | Residue |
| B | MET71 |
| B | ASN231 |
| B | ILE234 |
| B | GLY235 |
| B | HEM397 |
| B | GOL398 |
| B | HOH435 |
| B | HOH498 |
| B | HOH529 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 400 |
| Chain | Residue |
| B | ALA6 |
| B | VAL7 |
| B | ASP8 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 401 |
| Chain | Residue |
| B | ASP269 |
| B | ARG352 |
| B | HOH449 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 402 |
| Chain | Residue |
| B | MET33 |
| B | HOH465 |
| B | HOH538 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGMHHCLG |
| Chain | Residue | Details |
| A | PHE338-GLY347 |
