1Z8P
Ferrous dioxygen complex of the A245S 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 | 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 | 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 | 24 |
Details | BINDING SITE FOR RESIDUE HEM A 410 |
Chain | Residue |
A | MET90 |
A | ARG293 |
A | SER343 |
A | PHE344 |
A | GLY345 |
A | ILE348 |
A | HIS349 |
A | CYS351 |
A | GLY353 |
A | ALA357 |
A | OXY417 |
A | GLY91 |
A | DEB420 |
A | HOH425 |
A | HOH426 |
A | HOH434 |
A | HOH435 |
A | HIS98 |
A | ARG102 |
A | PHE109 |
A | ALA241 |
A | GLY242 |
A | SER245 |
A | PRO288 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OXY A 417 |
Chain | Residue |
A | ALA241 |
A | SER245 |
A | HEM410 |
A | DEB420 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE DEB A 420 |
Chain | Residue |
A | ALA74 |
A | GLY91 |
A | THR92 |
A | ILE174 |
A | VAL237 |
A | LEU392 |
A | HEM410 |
A | OXY417 |
A | HOH421 |
A | HOH430 |
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 | 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 |