Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | LEU90 |
| A | GLN251 |
| A | LEU284 |
| A | THR289 |
| A | LEU290 |
| A | THR293 |
| A | ARG296 |
| A | ALA347 |
| A | PHE348 |
| A | GLY349 |
| A | GLY350 |
| A | GLN91 |
| A | HIS353 |
| A | CYS355 |
| A | GLY357 |
| A | LEU360 |
| A | GLU364 |
| B | HOH434 |
| B | HOH441 |
| B | HOH562 |
| B | HOH723 |
| A | HIS98 |
| A | ARG102 |
| A | PHE109 |
| A | ALA243 |
| A | GLY244 |
| A | THR247 |
| A | THR248 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | LEU90 |
| B | GLN91 |
| B | HIS98 |
| B | ARG102 |
| B | PHE109 |
| B | ALA243 |
| B | GLY244 |
| B | THR247 |
| B | THR248 |
| B | LEU284 |
| B | THR289 |
| B | LEU290 |
| B | THR293 |
| B | ARG296 |
| B | ALA347 |
| B | PHE348 |
| B | GLY349 |
| B | GLY350 |
| B | HIS353 |
| B | CYS355 |
| B | LEU356 |
| B | GLY357 |
| B | LEU360 |
| B | ALA361 |
| B | HOH615 |
| B | HOH641 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 407 |
| Chain | Residue |
| A | ARG60 |
| A | PHE223 |
| A | GLY351 |
| A | PRO352 |
| A | EPE409 |
| B | HOH529 |
| B | HOH541 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 408 |
| Chain | Residue |
| A | ALA5 |
| A | HIS6 |
| A | THR7 |
| B | ARG69 |
| B | HOH721 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 407 |
| Chain | Residue |
| A | ARG69 |
| B | ALA5 |
| B | HIS6 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE EPE A 409 |
| Chain | Residue |
| A | HIS98 |
| A | ARG99 |
| A | ARG102 |
| A | PHE223 |
| A | HIS224 |
| A | GLY351 |
| A | PRO352 |
| A | PHE354 |
| A | SO4407 |
| B | HOH426 |
| B | HOH499 |
| B | HOH736 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EPE B 408 |
| Chain | Residue |
| B | HIS98 |
| B | ARG99 |
| B | ARG102 |
| B | PHE223 |
| B | HIS224 |
| B | GLY351 |
| B | PRO352 |
| B | PHE354 |
| B | HOH429 |
| B | HOH717 |
| B | HOH746 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 409 |
| Chain | Residue |
| B | ARG69 |
| B | ARG112 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGPHFCLG |
| Chain | Residue | Details |
| A | PHE348-GLY357 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS98 | |
| B | HIS98 | |
| Chain | Residue | Details |
| A | ARG102 | |
| A | ARG296 | |
| A | GLY350 | |
| A | HIS353 | |
| B | ARG102 | |
| B | ARG296 | |
| B | GLY350 | |
| B | HIS353 | |
| Chain | Residue | Details |
| A | CYS355 | |
| B | CYS355 | |
