2ZAX
Crystal Structure of Ferric 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 415 |
| Chain | Residue |
| A | GLU84 |
| A | GLY93 |
| A | GLU94 |
| A | TYR96 |
| A | HOH806 |
| A | HOH813 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 417 |
| Chain | Residue |
| 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 | GLY359 |
| A | CAM422 |
| A | HOH437 |
| A | HOH659 |
| A | PRO100 |
| A | THR101 |
| A | GLN108 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAM A 422 |
| Chain | Residue |
| A | PHE87 |
| A | TYR96 |
| A | LEU244 |
| A | VAL295 |
| A | HEM417 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS A 423 |
| Chain | Residue |
| A | HIS21 |
| A | VAL23 |
| A | PHE24 |
| A | ASN49 |
| A | VAL50 |
| A | PRO51 |
| A | HOH802 |
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 |
