1QMQ
Optical detection of cytochrome P450 by sensitizer-linked substrates
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein 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 | 0018683 | molecular_function | camphor 5-monooxygenase activity |
A | 0019383 | biological_process | (+)-camphor catabolic 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 421 |
Chain | Residue |
A | SER267 |
A | PRO268 |
A | GLU269 |
A | HIS270 |
A | HOH2423 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 422 |
Chain | Residue |
A | GLN360 |
A | HIS361 |
A | HOH2169 |
A | HOH2424 |
A | ARG112 |
A | ASP188 |
A | LEU356 |
A | CYS357 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACT A 423 |
Chain | Residue |
A | LEU45 |
A | GLN46 |
A | GLU47 |
A | VAL50 |
A | PRO51 |
A | ASP52 |
A | THR66 |
A | ARG67 |
A | ARG330 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 424 |
Chain | Residue |
A | MET184 |
A | PHE193 |
A | DRB418 |
A | DRB419 |
A | HOH2425 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 425 |
Chain | Residue |
A | ARG271 |
A | GLN272 |
A | PRO379 |
A | ASP380 |
site_id | AC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM A 417 |
Chain | Residue |
A | PRO100 |
A | THR101 |
A | GLN108 |
A | ARG112 |
A | LEU245 |
A | GLY248 |
A | GLY249 |
A | THR252 |
A | ASP297 |
A | ARG299 |
A | GLN322 |
A | THR349 |
A | PHE350 |
A | GLY351 |
A | HIS355 |
A | CYS357 |
A | GLY359 |
A | DRB419 |
A | HOH2146 |
A | HOH2285 |
A | HOH2420 |
A | HOH2421 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE LRB A 418 |
Chain | Residue |
A | TYR29 |
A | TYR96 |
A | THR101 |
A | THR185 |
A | ARG186 |
A | PRO187 |
A | GLY248 |
A | ASP297 |
A | ILE395 |
A | ACT424 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE DRB A 419 |
Chain | Residue |
A | TYR29 |
A | ASN59 |
A | PHE87 |
A | ILE88 |
A | PRO89 |
A | ALA92 |
A | TYR96 |
A | THR101 |
A | PRO187 |
A | GLY248 |
A | ASP297 |
A | ILE395 |
A | HEM417 |
A | ACT424 |
A | HOH2285 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGSHLCLG |
Chain | Residue | Details |
A | PHE350-GLY359 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | LEU358 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1akd |
Chain | Residue | Details |
A | ASP251 | |
A | THR252 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 133 |
Chain | Residue | Details |
A | PRO187 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | VAL253 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | LEU358 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
A | GLY359 | electrostatic stabiliser, hydrogen bond donor |
A | GLN360 | electrostatic stabiliser, hydrogen bond donor |