3FWF
Ferric camphor bound cytochrome P450cam containing a Selenocysteine as the 5th heme ligand, monoclinic crystal form
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 | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| 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 | 0006707 | biological_process | cholesterol catabolic process |
| B | 0008395 | molecular_function | steroid hydroxylase 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 417 |
| Chain | Residue |
| A | PRO100 |
| A | ASP297 |
| A | ARG299 |
| A | GLN322 |
| A | THR349 |
| A | PHE350 |
| A | GLY351 |
| A | HIS355 |
| A | SEC357 |
| A | LEU358 |
| A | CAM420 |
| A | THR101 |
| A | HOH614 |
| A | GLN108 |
| A | ARG112 |
| A | LEU244 |
| A | LEU245 |
| A | THR252 |
| A | VAL253 |
| A | LEU294 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAM A 420 |
| Chain | Residue |
| A | PHE87 |
| A | TYR96 |
| A | LEU244 |
| A | VAL295 |
| A | HEM417 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 515 |
| Chain | Residue |
| A | GLU84 |
| A | GLY93 |
| A | GLU94 |
| A | TYR96 |
| A | HOH430 |
| A | HOH467 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 515 |
| Chain | Residue |
| B | GLU84 |
| B | GLY93 |
| B | GLU94 |
| B | TYR96 |
| B | HOH519 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM B 417 |
| Chain | Residue |
| B | PRO100 |
| B | THR101 |
| B | GLN108 |
| B | ARG112 |
| B | LEU245 |
| B | GLY248 |
| B | GLY249 |
| B | THR252 |
| B | ASP297 |
| B | ARG299 |
| B | GLN322 |
| B | THR349 |
| B | PHE350 |
| B | GLY351 |
| B | HIS355 |
| B | SEC357 |
| B | LEU358 |
| B | CAM420 |
| B | HOH676 |
| B | HOH782 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAM B 420 |
| Chain | Residue |
| B | PHE87 |
| B | TYR96 |
| B | LEU244 |
| B | VAL295 |
| B | HEM417 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 715 |
| Chain | Residue |
| B | HOH8 |
| B | LEU14 |
| B | PRO15 |
| B | PRO16 |
| B | VAL18 |
| B | GLU20 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 716 |
| Chain | Residue |
| B | PRO105 |
| B | PRO106 |
| B | GLN108 |
| B | ARG109 |
| B | HOH541 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | SEC357 | |
| B | SEC357 |
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 | SEC357 | 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 | SEC357 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| B | LEU358 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY359 | electrostatic stabiliser, hydrogen bond donor |
