1Z8Q
Ferrous dioxygen complex of the A245T 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 | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| 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 | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 410 |
| Chain | Residue |
| A | MET90 |
| A | SER343 |
| A | GLY345 |
| A | ILE348 |
| A | HIS349 |
| A | CYS351 |
| A | ALA357 |
| A | OXY417 |
| A | DEB420 |
| A | HOH425 |
| A | HOH431 |
| A | GLY91 |
| A | HOH440 |
| A | HOH463 |
| A | HIS98 |
| A | ARG102 |
| A | PHE109 |
| A | ALA241 |
| A | GLY242 |
| A | THR245 |
| A | ARG293 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OXY A 417 |
| Chain | Residue |
| A | ALA241 |
| A | THR245 |
| A | HEM410 |
| A | DEB420 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DEB A 420 |
| Chain | Residue |
| A | ALA74 |
| A | GLY91 |
| A | THR92 |
| A | ILE174 |
| A | LEU175 |
| A | VAL237 |
| A | THR245 |
| A | LEU391 |
| A | LEU392 |
| A | HEM410 |
| A | OXY417 |
| A | HOH422 |
| A | HOH433 |
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: axial binding residue => ECO:0000269|PubMed:10716705, ECO:0000269|PubMed:11469860, ECO:0000269|PubMed:15824115, ECO:0000269|PubMed:7749919 |
| Chain | Residue | Details |
| A | CYS351 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | THR245 | |
| A | GLU244 |
| 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 |
