1RE9
CRYSTAL STRUCTURE OF CYTOCHROME P450-CAM WITH A FLUORESCENT PROBE D-8-AD (ADAMANTANE-1-CARBOXYLIC ACID-5-DIMETHYLAMINO-NAPHTHALENE-1-SULFONYLAMINO-OCTYL-AMIDE)
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 801 |
| Chain | Residue |
| A | GLU74 |
| A | GLY83 |
| A | GLU84 |
| A | TYR86 |
| A | HOH942 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | LEU234 |
| A | LEU235 |
| A | GLY238 |
| A | GLY239 |
| A | THR242 |
| A | ASP287 |
| A | ARG289 |
| A | GLN312 |
| A | THR339 |
| A | PHE340 |
| A | GLY341 |
| A | HIS345 |
| A | CYS347 |
| A | GLY349 |
| A | DSO601 |
| A | HOH807 |
| A | HOH817 |
| A | PRO90 |
| A | THR91 |
| A | GLN98 |
| A | ARG102 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DSO A 601 |
| Chain | Residue |
| A | TYR19 |
| A | PHE77 |
| A | PRO79 |
| A | TYR86 |
| A | PRO177 |
| A | PHE183 |
| A | VAL237 |
| A | ILE385 |
| A | HEM501 |
| A | HOH979 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 701 |
| Chain | Residue |
| A | GLU319 |
| A | ARG320 |
| A | GLU363 |
| A | ARG367 |
| A | HOH887 |
| A | HOH1071 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 702 |
| Chain | Residue |
| A | LEU264 |
| A | PRO268 |
| A | LYS362 |
| A | THR366 |
| A | HOH858 |
| A | HOH968 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 704 |
| Chain | Residue |
| A | VAL335 |
| A | SER336 |
| A | HIS337 |
| A | HOH1024 |
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 | PHE340-GLY349 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | THR242 | |
| A | ASP241 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 133 |
| Chain | Residue | Details |
| A | ARG176 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ASP241 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | THR242 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | CYS347 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| A | LEU348 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY349 | electrostatic stabiliser, hydrogen bond donor |
