1C8J
CRYSTAL STRUCTURE OF CYTOCHROME P450CAM MUTANT (F87W/Y96F)
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 | 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 | 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 | 0016491 | molecular_function | oxidoreductase 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 | CYS357 |
A | GLY359 |
A | HOH486 |
A | THR101 |
A | HOH490 |
A | GLN108 |
A | ARG112 |
A | LEU244 |
A | LEU245 |
A | GLY248 |
A | GLY249 |
A | THR252 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM B 417 |
Chain | Residue |
B | PRO100 |
B | THR101 |
B | GLN108 |
B | ARG112 |
B | PHE163 |
B | LEU244 |
B | LEU245 |
B | GLY248 |
B | GLY249 |
B | THR252 |
B | VAL295 |
B | ASP297 |
B | ARG299 |
B | GLN322 |
B | THR349 |
B | PHE350 |
B | GLY351 |
B | HIS355 |
B | CYS357 |
B | GLY359 |
B | HOH435 |
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 | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | LEU358 | |
B | LEU358 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 133 |
Chain | Residue | Details |
A | PRO187 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | VAL253 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | LEU358 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
A | GLY359 | electrostatic stabiliser, hydrogen bond donor |
A | GLN360 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 133 |
Chain | Residue | Details |
B | PRO187 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | VAL253 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | LEU358 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
B | GLY359 | electrostatic stabiliser, hydrogen bond donor |
B | GLN360 | electrostatic stabiliser, hydrogen bond donor |