5L91
The 2.2 A crystal structure of CYP109E1 from Bacillus megaterium bound with four corticosterone molecules
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 | 26 |
| 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 | LEU357 |
| A | ALA358 |
| A | C0R502 |
| A | HOH610 |
| A | HOH616 |
| A | HOH622 |
| A | HOH648 |
| A | HIS92 |
| A | ARG96 |
| A | LEU239 |
| A | ALA242 |
| A | GLY243 |
| A | THR246 |
| A | THR247 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue C0R A 502 |
| Chain | Residue |
| A | ILE85 |
| A | ILE168 |
| A | VAL169 |
| A | LYS187 |
| A | ILE241 |
| A | GLU245 |
| A | VAL289 |
| A | LEU292 |
| A | VAL392 |
| A | HEM501 |
| A | C0R503 |
| A | C0R504 |
| A | C0R505 |
| A | HOH622 |
| A | HOH707 |
| B | ARG177 |
| B | GLU178 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue C0R A 503 |
| Chain | Residue |
| A | ARG69 |
| A | PRO71 |
| A | GLN75 |
| A | ASN86 |
| A | ILE241 |
| A | C0R502 |
| A | C0R504 |
| A | C0R505 |
| B | GLU181 |
| B | GLN185 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue C0R A 504 |
| Chain | Residue |
| A | ARG44 |
| A | VAL46 |
| A | ARG69 |
| A | LEU292 |
| A | HIS293 |
| A | HIS312 |
| A | PHE391 |
| A | C0R502 |
| A | C0R503 |
| A | C0R505 |
| A | HOH610 |
| B | LYS182 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue C0R A 505 |
| Chain | Residue |
| A | ARG76 |
| A | GLN184 |
| A | MET188 |
| A | ASN191 |
| A | C0R502 |
| A | C0R503 |
| A | C0R504 |
| B | GLU181 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | LEU84 |
| B | ILE85 |
| B | HIS92 |
| B | ARG96 |
| B | LEU239 |
| 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 | ALA358 |
| B | C0R502 |
| B | HOH610 |
| B | HOH626 |
| B | HOH630 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue C0R B 502 |
| Chain | Residue |
| B | LYS187 |
| B | ILE241 |
| B | GLU245 |
| B | THR246 |
| B | VAL289 |
| B | LEU292 |
| B | VAL392 |
| B | HEM501 |
| B | C0R503 |
| B | C0R504 |
| B | C0R505 |
| B | HOH610 |
| B | HOH653 |
| A | ARG177 |
| B | ILE85 |
| B | ILE168 |
| B | VAL169 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue C0R B 503 |
| Chain | Residue |
| A | GLU181 |
| A | GLN185 |
| B | ARG69 |
| B | PRO71 |
| B | GLN75 |
| B | LEU80 |
| B | GLY81 |
| B | ASN86 |
| B | ILE241 |
| B | C0R502 |
| B | C0R504 |
| B | C0R505 |
| B | HOH650 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue C0R B 504 |
| Chain | Residue |
| A | LYS182 |
| B | ARG44 |
| B | VAL46 |
| B | ARG69 |
| B | LEU292 |
| B | HIS293 |
| B | HIS312 |
| B | PHE391 |
| B | C0R502 |
| B | C0R503 |
| B | C0R505 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue C0R B 505 |
| Chain | Residue |
| A | GLU181 |
| B | ARG76 |
| B | MET188 |
| B | ASN191 |
| B | C0R502 |
| B | C0R503 |
| B | C0R504 |
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 |
