5CP4
CRYOGENIC STRUCTURE OF 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 | 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 500 |
Chain | Residue |
A | GLU84 |
A | GLY93 |
A | GLU94 |
A | TYR96 |
A | HOH767 |
A | HOH852 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEM A 417 |
Chain | Residue |
A | ARG112 |
A | LEU245 |
A | GLY248 |
A | GLY249 |
A | THR252 |
A | VAL295 |
A | ASP297 |
A | ARG299 |
A | GLN322 |
A | THR349 |
A | PHE350 |
A | GLY351 |
A | HIS355 |
A | CYS357 |
A | CAM422 |
A | HOH511 |
A | HOH652 |
A | HOH725 |
A | PRO100 |
A | THR101 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CAM A 422 |
Chain | Residue |
A | PHE87 |
A | TYR96 |
A | LEU244 |
A | HEM417 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 491 |
Chain | Residue |
A | MET121 |
A | ASP125 |
A | PRO175 |
A | HIS176 |
A | ARG365 |
A | HOH876 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 492 |
Chain | Residue |
A | PRO19 |
A | HIS21 |
A | CYS136 |
A | GLU140 |
A | ARG377 |
A | VAL414 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 493 |
Chain | Residue |
A | SER267 |
A | PRO268 |
A | GLU269 |
A | HIS270 |
site_id | K |
Number of Residues | 1 |
Details | POTASSIUM BINDING SITE. |
Chain | Residue |
A | K500 |
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: axial binding residue |
Chain | Residue | Details |
A | LEU358 |
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 | 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 |