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 | 0020037 | molecular_function | heme binding |
| A | 0033072 | biological_process | vancomycin biosynthetic process |
| 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 | 0020037 | molecular_function | heme binding |
| B | 0033072 | biological_process | vancomycin biosynthetic process |
| 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 1430 |
| Chain | Residue |
| A | ILE97 |
| A | VAL292 |
| A | PRO295 |
| A | ARG298 |
| A | ILE321 |
| A | GLY348 |
| A | PHE349 |
| A | ILE353 |
| A | HIS354 |
| A | CYS356 |
| A | ALA362 |
| A | SER98 |
| A | PG44502 |
| A | HOH4514 |
| A | HOH4518 |
| A | HOH4606 |
| A | HOH4693 |
| A | HIS105 |
| A | ARG109 |
| A | PHE116 |
| A | GLY245 |
| A | GLY246 |
| A | THR249 |
| A | MET253 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PG4 A 4502 |
| Chain | Residue |
| A | GLN96 |
| A | SER98 |
| A | THR99 |
| A | ALA241 |
| A | GLY245 |
| A | ASN296 |
| A | HEM1430 |
| A | HOH4518 |
| A | HOH4611 |
| A | HOH4635 |
| A | HOH4654 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM B 2430 |
| Chain | Residue |
| B | ILE97 |
| B | SER98 |
| B | HIS105 |
| B | ARG109 |
| B | PHE116 |
| B | LEU161 |
| B | GLY245 |
| B | GLY246 |
| B | THR249 |
| B | VAL250 |
| B | VAL292 |
| B | PRO295 |
| B | ARG298 |
| B | ILE321 |
| B | GLY348 |
| B | PHE349 |
| B | GLY350 |
| B | ILE353 |
| B | HIS354 |
| B | CYS356 |
| B | ALA362 |
| B | PG45502 |
| B | HOH5505 |
| B | HOH5608 |
| B | HOH5669 |
| B | HOH5680 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PG4 B 5502 |
| Chain | Residue |
| B | PHE93 |
| B | GLN96 |
| B | SER98 |
| B | ALA241 |
| B | GLY245 |
| B | ASN296 |
| B | HEM2430 |
| B | HOH5622 |
| B | HOH5680 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 4503 |
| Chain | Residue |
| A | PHE272 |
| A | TRP374 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHYCVG |
| Chain | Residue | Details |
| A | PHE349-GLY358 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12888556","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UED","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | GLU248 | |
| A | THR249 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | GLU248 | |
| B | THR249 | |
