1Z8O
Ferrous dioxygen complex of the wild-type cytochrome P450eryF
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| A | 1901115 | biological_process | erythromycin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 410 |
| Chain | Residue |
| A | MET90 |
| A | SER343 |
| A | PHE344 |
| A | GLY345 |
| A | ILE348 |
| A | HIS349 |
| A | CYS351 |
| A | GLY353 |
| A | ALA357 |
| A | OXY417 |
| A | DEB420 |
| A | GLY91 |
| A | HOH422 |
| A | HOH427 |
| A | HOH432 |
| A | HOH446 |
| A | HIS98 |
| A | ARG102 |
| A | PHE109 |
| A | GLY242 |
| A | ALA245 |
| A | PRO288 |
| A | ARG293 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OXY A 417 |
| Chain | Residue |
| A | ALA241 |
| A | HEM410 |
| A | DEB420 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DEB A 420 |
| Chain | Residue |
| A | ALA74 |
| A | GLY91 |
| A | THR92 |
| A | ILE174 |
| A | LEU175 |
| A | VAL237 |
| A | LEU392 |
| A | HEM410 |
| A | OXY417 |
| A | HOH423 |
| A | HOH428 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGqGIHFCMG |
| Chain | Residue | Details |
| A | PHE344-GLY353 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10716705","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11469860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15824115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7749919","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 694 |
| Chain | Residue | Details |
| A | ALA241 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | GLU244 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | SER246 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor, proton relay |
| A | CYS351 | covalently attached, metal ligand |
| A | GLU360 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
