Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| A | 0140825 | molecular_function | lactoperoxidase activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| 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 |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0140825 | molecular_function | lactoperoxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue 3SQ A 401 |
| Chain | Residue |
| A | ALA152 |
| A | LEU155 |
| A | GLY156 |
| A | ALA209 |
| A | VAL353 |
| A | LEU354 |
| A | HEM402 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue HEM A 402 |
| Chain | Residue |
| A | HIS76 |
| A | ARG80 |
| A | PHE87 |
| A | LEU205 |
| A | LEU206 |
| A | GLY210 |
| A | THR213 |
| A | THR214 |
| A | LEU217 |
| A | THR257 |
| A | ARG259 |
| A | SER309 |
| A | PHE310 |
| A | GLY311 |
| A | ILE314 |
| A | HIS315 |
| A | CYS317 |
| A | GLY319 |
| A | ALA323 |
| A | 3SQ401 |
| A | HOH595 |
| A | HOH598 |
| A | HOH706 |
| A | MET68 |
| A | LEU69 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue HEM B 401 |
| Chain | Residue |
| B | MET68 |
| B | LEU69 |
| B | HIS76 |
| B | ARG80 |
| B | PHE87 |
| B | LEU205 |
| B | LEU206 |
| B | GLY210 |
| B | THR213 |
| B | THR214 |
| B | LEU217 |
| B | THR257 |
| B | ARG259 |
| B | SER309 |
| B | PHE310 |
| B | GLY311 |
| B | ILE314 |
| B | HIS315 |
| B | CYS317 |
| B | GLY319 |
| B | ALA323 |
| B | 3SQ402 |
| B | HOH604 |
| B | HOH614 |
| B | HOH724 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue 3SQ B 402 |
| Chain | Residue |
| B | ALA152 |
| B | LEU155 |
| B | GLY156 |
| B | ALA209 |
| B | VAL353 |
| B | LEU354 |
| B | HEM401 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGIHLCLG |
| Chain | Residue | Details |
| A | PHE310-GLY319 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS76 | |
| B | HIS315 | |
| A | ARG80 | |
| A | THR257 | |
| A | ARG259 | |
| A | HIS315 | |
| B | HIS76 | |
| B | ARG80 | |
| B | THR257 | |
| B | ARG259 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS317 | |
| B | CYS317 | |
