2QBM
Crystal structure of the P450cam G248T mutant in the cyanide bound state
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 | 3 |
| Details | BINDING SITE FOR RESIDUE CYN A 421 |
| Chain | Residue |
| A | THR252 |
| A | HEM516 |
| A | CAM517 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 515 |
| Chain | Residue |
| A | GLU84 |
| A | GLY93 |
| A | GLU94 |
| A | TYR96 |
| A | HOH634 |
| A | HOH779 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 516 |
| Chain | Residue |
| A | THR101 |
| A | GLN108 |
| A | ARG112 |
| A | VAL119 |
| A | THR248 |
| A | THR252 |
| A | VAL253 |
| A | LEU294 |
| A | ASP297 |
| A | ARG299 |
| A | GLN322 |
| A | THR349 |
| A | PHE350 |
| A | GLY351 |
| A | HIS355 |
| A | CYS357 |
| A | GLY359 |
| A | LEU362 |
| A | CYN421 |
| A | CAM517 |
| A | HOH520 |
| A | HOH604 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CAM A 517 |
| Chain | Residue |
| A | PHE87 |
| A | TYR96 |
| A | THR101 |
| A | THR248 |
| A | VAL295 |
| A | ASP297 |
| A | CYN421 |
| A | HEM516 |
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 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 | ASP251 | |
| A | 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 |
