1K2O
Cytochrome P450Cam with Bound BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II)
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 | 0016491 | molecular_function | oxidoreductase 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 | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0018683 | molecular_function | camphor 5-monooxygenase activity |
| B | 0019383 | biological_process | (+)-camphor catabolic process |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CAC B 500 |
| Chain | Residue |
| B | GLU84 |
| B | CYS85 |
| B | PHE87 |
| B | ARG90 |
| B | GLY93 |
| B | GLU94 |
| B | TYR96 |
| B | SER102 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CAC A 501 |
| Chain | Residue |
| A | ARG90 |
| A | GLY93 |
| A | TYR96 |
| A | CYS85 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAC B 502 |
| Chain | Residue |
| B | ALA9 |
| B | ASN10 |
| B | LEU11 |
| B | ASP27 |
| B | CYS58 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CAC A 503 |
| Chain | Residue |
| A | ASN10 |
| A | LEU11 |
| A | ASP27 |
| A | CYS58 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CAC B 504 |
| Chain | Residue |
| B | GLU133 |
| B | CYS136 |
| B | SER137 |
| B | GLU140 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 417 |
| Chain | Residue |
| A | PRO100 |
| A | GLN108 |
| A | ARG112 |
| A | LEU244 |
| 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 | LEU358 |
| A | GLY359 |
| A | RFA900 |
| A | RFB901 |
| A | HOH1015 |
| A | HOH1063 |
| A | HOH1164 |
| A | HOH1366 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 417 |
| Chain | Residue |
| B | PRO100 |
| B | GLN108 |
| B | ARG112 |
| B | LEU244 |
| B | LEU245 |
| B | GLY248 |
| B | GLY249 |
| B | THR252 |
| B | ASP297 |
| B | ARG299 |
| B | GLN322 |
| B | THR349 |
| B | PHE350 |
| B | GLY351 |
| B | HIS355 |
| B | CYS357 |
| B | GLY359 |
| B | RFA902 |
| B | RFB903 |
| B | HOH1204 |
| B | HOH1324 |
| B | HOH1327 |
| B | HOH1689 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE RFA A 900 |
| Chain | Residue |
| A | PHE87 |
| A | PRO89 |
| A | ALA92 |
| A | GLY93 |
| A | GLU94 |
| A | TYR96 |
| A | MET184 |
| A | THR185 |
| A | PRO187 |
| A | PHE193 |
| A | VAL247 |
| A | ASP297 |
| A | ILE395 |
| A | VAL396 |
| A | HEM417 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE RFB A 901 |
| Chain | Residue |
| A | VAL396 |
| A | HEM417 |
| A | TYR29 |
| A | PHE87 |
| A | ALA92 |
| A | GLY93 |
| A | GLU94 |
| A | TYR96 |
| A | MET184 |
| A | THR185 |
| A | PHE193 |
| A | LEU244 |
| A | VAL247 |
| A | ILE395 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE RFA B 902 |
| Chain | Residue |
| B | PHE87 |
| B | PRO89 |
| B | ALA92 |
| B | GLY93 |
| B | GLU94 |
| B | TYR96 |
| B | MET184 |
| B | THR185 |
| B | PRO187 |
| B | PHE193 |
| B | VAL247 |
| B | ILE395 |
| B | VAL396 |
| B | HEM417 |
| B | HOH1415 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE RFB B 903 |
| Chain | Residue |
| B | PHE87 |
| B | ALA92 |
| B | GLY93 |
| B | GLU94 |
| B | TYR96 |
| B | MET184 |
| B | THR185 |
| B | PRO187 |
| B | GLY189 |
| B | PHE193 |
| B | VAL247 |
| B | ILE395 |
| B | HEM417 |
| B | HOH1415 |
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 | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | LEU358 | |
| B | 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 | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | ASP251 | |
| B | THR252 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 133 |
| Chain | Residue | Details |
| A | ARG186 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ASP251 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | CYS357 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| A | LEU358 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY359 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 133 |
| Chain | Residue | Details |
| B | ARG186 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | ASP251 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | CYS357 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| B | LEU358 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY359 | electrostatic stabiliser, hydrogen bond donor |
