2QBL
Crystal structure of ferric G248T cytochrome P450cam
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 | 6 | 
| Details | BINDING SITE FOR RESIDUE K A 515 | 
| Chain | Residue | 
| A | GLU84 | 
| A | GLY93 | 
| A | GLU94 | 
| A | TYR96 | 
| A | HOH634 | 
| A | HOH787 | 
| site_id | AC2 | 
| Number of Residues | 18 | 
| Details | BINDING SITE FOR RESIDUE HEM A 516 | 
| Chain | Residue | 
| A | ARG112 | 
| A | VAL119 | 
| A | THR248 | 
| A | THR252 | 
| A | ASP297 | 
| A | ARG299 | 
| A | THR349 | 
| A | PHE350 | 
| A | GLY351 | 
| A | HIS355 | 
| A | CYS357 | 
| A | GLY359 | 
| A | LEU362 | 
| A | CAM517 | 
| A | HOH520 | 
| A | PRO100 | 
| A | THR101 | 
| A | GLN108 | 
| site_id | AC3 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE CAM A 517 | 
| Chain | Residue | 
| A | PHE87 | 
| A | TYR96 | 
| A | THR248 | 
| A | VAL295 | 
| 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 | 






