5L92
The 2.1 A crystal structure of CYP109E1 from Bacillus megaterium in complex with corticosterone
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 | 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 | 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 | 24 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | LEU84 |
| A | LEU250 |
| A | LEU292 |
| A | ARG294 |
| A | ALA344 |
| A | PHE345 |
| A | GLY346 |
| A | ILE349 |
| A | HIS350 |
| A | CYS352 |
| A | GLY354 |
| A | ILE85 |
| A | ALA358 |
| A | C0R502 |
| A | MLA503 |
| A | HOH613 |
| A | HOH629 |
| A | HIS92 |
| A | ARG96 |
| A | LEU238 |
| A | LEU239 |
| A | ALA242 |
| A | THR246 |
| A | THR247 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue C0R A 502 |
| Chain | Residue |
| A | ILE168 |
| A | LEU238 |
| A | ILE241 |
| A | ALA242 |
| A | PHE391 |
| A | HEM501 |
| A | MLA503 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue MLA A 503 |
| Chain | Residue |
| A | ARG69 |
| A | ILE85 |
| A | LEU292 |
| A | HIS293 |
| A | ARG294 |
| A | PHE391 |
| A | HEM501 |
| A | C0R502 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | LEU84 |
| B | ILE85 |
| B | HIS92 |
| B | ARG96 |
| B | ILE147 |
| B | ALA242 |
| B | GLY243 |
| B | THR246 |
| B | THR247 |
| B | LEU292 |
| B | ARG294 |
| B | ALA344 |
| B | PHE345 |
| B | GLY346 |
| B | ILE349 |
| B | HIS350 |
| B | CYS352 |
| B | GLY354 |
| B | LEU357 |
| B | ALA358 |
| B | HOH617 |
| B | HOH619 |
| B | HOH624 |
| B | HOH632 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGIHFCLG |
| Chain | Residue | Details |
| A | PHE345-GLY354 |
