5OFQ
Crystal structure of substrate-free CYP109A2 from Bacillus megaterium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| 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 | 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 | 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 |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | ILE83 |
| A | THR246 |
| A | LEU282 |
| A | ILE291 |
| A | ARG293 |
| A | SER343 |
| A | PHE344 |
| A | GLY345 |
| A | HIS349 |
| A | CYS351 |
| A | GLY353 |
| A | LEU84 |
| A | ALA357 |
| A | HIS91 |
| A | ARG95 |
| A | ILE146 |
| A | LEU237 |
| A | ALA241 |
| A | GLY242 |
| A | THR245 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE A 502 |
| Chain | Residue |
| A | TYR29 |
| A | GLU259 |
| A | TYR285 |
| B | SO4503 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE A 503 |
| Chain | Residue |
| A | LYS198 |
| A | GLN206 |
| C | ARG105 |
| D | GLU327 |
| D | VAL333 |
| D | HIS335 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | LYS61 |
| A | LYS65 |
| A | PHE346 |
| D | ARG308 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | THR103 |
| A | ARG105 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | ILE83 |
| B | LEU84 |
| B | HIS91 |
| B | ARG95 |
| B | ILE146 |
| B | LEU237 |
| B | ALA241 |
| B | GLY242 |
| B | THR245 |
| B | THR246 |
| B | LEU249 |
| B | ILE291 |
| B | ARG293 |
| B | SER343 |
| B | PHE344 |
| B | GLY345 |
| B | HIS349 |
| B | CYS351 |
| B | GLY353 |
| B | ALA357 |
| B | HOH601 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE B 502 |
| Chain | Residue |
| A | ARG105 |
| B | TYR29 |
| B | TYR256 |
| B | GLU259 |
| B | ASP260 |
| B | TYR284 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| A | 1PE502 |
| B | THR103 |
| B | ARG105 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE C 501 |
| Chain | Residue |
| A | GLU116 |
| A | TYR120 |
| A | GLU148 |
| C | LYS65 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE C 502 |
| Chain | Residue |
| A | ARG204 |
| A | GLN209 |
| C | ASN339 |
| C | HIS341 |
| C | PHE350 |
| C | ARG358 |
| site_id | AD2 |
| Number of Residues | 20 |
| Details | binding site for residue HEM C 503 |
| Chain | Residue |
| C | ILE83 |
| C | LEU84 |
| C | HIS91 |
| C | ARG95 |
| C | ILE146 |
| C | LEU237 |
| C | ALA241 |
| C | GLY242 |
| C | THR245 |
| C | THR246 |
| C | ILE291 |
| C | ARG293 |
| C | SER343 |
| C | PHE344 |
| C | GLY345 |
| C | HIS349 |
| C | CYS351 |
| C | GLY353 |
| C | LEU356 |
| C | ALA357 |
| site_id | AD3 |
| Number of Residues | 21 |
| Details | binding site for residue HEM D 501 |
| Chain | Residue |
| D | ARG95 |
| D | ILE146 |
| D | LEU238 |
| D | ALA241 |
| D | GLY242 |
| D | THR245 |
| D | THR246 |
| D | LEU249 |
| D | ILE291 |
| D | ARG293 |
| D | SER343 |
| D | PHE344 |
| D | GLY345 |
| D | ILE348 |
| D | HIS349 |
| D | CYS351 |
| D | GLY353 |
| D | ALA357 |
| D | ILE83 |
| D | LEU84 |
| D | HIS91 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGIHFCLG |
| Chain | Residue | Details |
| A | PHE344-GLY353 |
