3W9C
Crystal structure of the electron transfer complex of cytochrome p450cam with putidaredoxin
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 | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0140647 | biological_process | P450-containing electron transport chain |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | GLN108 |
| A | ARG299 |
| A | GLN322 |
| A | THR349 |
| A | PHE350 |
| A | GLY351 |
| A | HIS355 |
| A | CYS357 |
| A | GLY359 |
| A | GOL505 |
| A | ARG112 |
| A | LEU244 |
| A | LEU245 |
| A | GLY248 |
| A | GLY249 |
| A | THR252 |
| A | PHE256 |
| A | ASP297 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | SER267 |
| A | PRO268 |
| A | GLU269 |
| A | HIS270 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | ALA334 |
| A | PRO335 |
| A | MET336 |
| A | HIS337 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 504 |
| Chain | Residue |
| A | PRO19 |
| A | GLU20 |
| A | HIS21 |
| A | ARG271 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 505 |
| Chain | Residue |
| A | GLY248 |
| A | THR252 |
| A | HEM501 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES B 201 |
| Chain | Residue |
| B | GLY37 |
| B | CYS39 |
| B | GLY41 |
| B | ALA43 |
| B | SER44 |
| B | CYS45 |
| B | ALA46 |
| B | CYS48 |
| B | CYS86 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 202 |
| Chain | Residue |
| B | HIS8 |
| B | ALA76 |
| B | GLU77 |
| B | ASP103 |
| B | ARG104 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:8204575 |
| Chain | Residue | Details |
| B | CYS39 | |
| B | CYS45 | |
| B | CYS48 | |
| B | CYS86 |
Catalytic Information from CSA
| 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 |
