4JX1
Crystal structure of reduced Cytochrome P450cam-putidaredoxin complex bound to camphor and 5-exo-hydroxycamphor
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 |
| 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 | 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 | 0046872 | molecular_function | metal ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0022900 | biological_process | electron transport chain |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0140647 | biological_process | P450-containing electron transport chain |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0022900 | biological_process | electron transport chain |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0140647 | biological_process | P450-containing electron transport chain |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| E | 0018683 | molecular_function | camphor 5-monooxygenase activity |
| E | 0019383 | biological_process | (+)-camphor catabolic process |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| F | 0018683 | molecular_function | camphor 5-monooxygenase activity |
| F | 0019383 | biological_process | (+)-camphor catabolic process |
| F | 0020037 | molecular_function | heme binding |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005515 | molecular_function | protein binding |
| G | 0005829 | cellular_component | cytosol |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0022900 | biological_process | electron transport chain |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051536 | molecular_function | iron-sulfur cluster binding |
| G | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| G | 0140647 | biological_process | P450-containing electron transport chain |
| H | 0005515 | molecular_function | protein binding |
| H | 0005829 | cellular_component | cytosol |
| H | 0009055 | molecular_function | electron transfer activity |
| H | 0022900 | biological_process | electron transport chain |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051536 | molecular_function | iron-sulfur cluster binding |
| H | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| H | 0140647 | biological_process | P450-containing electron transport chain |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | PRO100 |
| A | ASP297 |
| A | ARG299 |
| A | GLN322 |
| A | THR349 |
| A | PHE350 |
| A | GLY351 |
| A | HIS355 |
| A | CYS357 |
| A | LEU358 |
| A | LEU362 |
| A | THR101 |
| A | ALA363 |
| A | CAH503 |
| A | HOH624 |
| A | HOH653 |
| A | HOH687 |
| A | HOH882 |
| A | GLN108 |
| A | ARG112 |
| A | LEU244 |
| A | LEU245 |
| A | GLY248 |
| A | GLY249 |
| A | THR252 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CAM A 502 |
| Chain | Residue |
| A | ALA92 |
| A | TYR96 |
| A | MET184 |
| A | CAH503 |
| A | HOH810 |
| A | HOH858 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CAH A 503 |
| Chain | Residue |
| A | TYR96 |
| A | ASP297 |
| A | VAL396 |
| A | HEM501 |
| A | CAM502 |
| A | HOH687 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 504 |
| Chain | Residue |
| A | GLU198 |
| A | ASP202 |
| B | ALA36 |
| B | HOH675 |
| B | HOH722 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | PRO100 |
| B | THR101 |
| B | GLN108 |
| B | ARG112 |
| B | LEU244 |
| B | GLY248 |
| B | GLY249 |
| B | THR252 |
| B | LEU294 |
| B | ASP297 |
| B | ARG299 |
| B | GLN322 |
| B | THR349 |
| B | PHE350 |
| B | GLY351 |
| B | HIS355 |
| B | CYS357 |
| B | LEU358 |
| B | CAM502 |
| B | HOH625 |
| B | HOH655 |
| B | HOH694 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CAM B 502 |
| Chain | Residue |
| B | TYR96 |
| B | GLY248 |
| B | VAL396 |
| B | HEM501 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| A | ALA36 |
| A | HOH643 |
| A | HOH676 |
| A | HOH767 |
| B | GLU198 |
| B | ASP202 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES C 201 |
| Chain | Residue |
| C | GLY37 |
| C | CYS39 |
| C | GLY41 |
| C | ALA43 |
| C | SER44 |
| C | CYS45 |
| C | ALA46 |
| C | CYS48 |
| C | CYS86 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES D 201 |
| Chain | Residue |
| D | GLY37 |
| D | CYS39 |
| D | GLY41 |
| D | ALA43 |
| D | SER44 |
| D | CYS45 |
| D | ALA46 |
| D | CYS48 |
| D | CYS86 |
| site_id | BC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM E 501 |
| Chain | Residue |
| E | GLY249 |
| E | THR252 |
| E | LEU294 |
| E | ASP297 |
| E | ARG299 |
| E | GLN322 |
| E | THR349 |
| E | PHE350 |
| E | GLY351 |
| E | HIS355 |
| E | CYS357 |
| E | LEU358 |
| E | ALA363 |
| E | CAH503 |
| E | HOH601 |
| E | HOH622 |
| E | HOH670 |
| E | HOH723 |
| E | PRO100 |
| E | THR101 |
| E | GLN108 |
| E | ARG112 |
| E | LEU244 |
| E | LEU245 |
| E | GLY248 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAM E 502 |
| Chain | Residue |
| E | TYR96 |
| E | MET184 |
| E | PHE193 |
| E | ILE395 |
| E | CAH503 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CAH E 503 |
| Chain | Residue |
| E | PHE87 |
| E | TYR96 |
| E | ASP297 |
| E | VAL396 |
| E | HEM501 |
| E | CAM502 |
| E | HOH601 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1N0 E 504 |
| Chain | Residue |
| E | CYS344 |
| E | HOH812 |
| G | CYS19 |
| G | GLY20 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 505 |
| Chain | Residue |
| E | GLU198 |
| E | ASP202 |
| E | HOH652 |
| E | HOH692 |
| F | ALA36 |
| F | HOH679 |
| site_id | BC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM F 501 |
| Chain | Residue |
| F | PRO100 |
| F | THR101 |
| F | GLN108 |
| F | ARG112 |
| F | LEU244 |
| F | LEU245 |
| F | GLY248 |
| F | GLY249 |
| F | THR252 |
| F | LEU294 |
| F | ASP297 |
| F | ARG299 |
| F | GLN322 |
| F | THR349 |
| F | PHE350 |
| F | GLY351 |
| F | HIS355 |
| F | CYS357 |
| F | LEU358 |
| F | CAH503 |
| F | HOH603 |
| F | HOH611 |
| F | HOH643 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAM F 502 |
| Chain | Residue |
| F | TYR96 |
| F | MET184 |
| F | THR185 |
| F | VAL247 |
| F | ILE395 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CAH F 503 |
| Chain | Residue |
| F | PHE87 |
| F | LEU244 |
| F | GLY248 |
| F | ASP297 |
| F | ILE395 |
| F | VAL396 |
| F | HEM501 |
| F | HOH643 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA F 504 |
| Chain | Residue |
| E | ALA36 |
| E | HOH650 |
| E | HOH679 |
| F | GLU198 |
| F | ASP202 |
| F | HOH632 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES G 201 |
| Chain | Residue |
| G | GLY37 |
| G | CYS39 |
| G | GLY41 |
| G | ALA43 |
| G | SER44 |
| G | CYS45 |
| G | ALA46 |
| G | CYS48 |
| G | CYS86 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES H 201 |
| Chain | Residue |
| H | GLY37 |
| H | CYS39 |
| H | GLY41 |
| H | ALA43 |
| H | SER44 |
| H | CYS45 |
| H | ALA46 |
| H | CYS48 |
| H | CYS86 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 416 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8204575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
| 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 | CYS357 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| B | LEU358 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY359 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 133 |
| Chain | Residue | Details |
| E | ARG186 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| E | ASP251 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| E | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| E | CYS357 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| E | LEU358 | electrostatic stabiliser, hydrogen bond donor |
| E | GLY359 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 133 |
| Chain | Residue | Details |
| F | ARG186 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| F | ASP251 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| F | THR252 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| F | CYS357 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand |
| F | LEU358 | electrostatic stabiliser, hydrogen bond donor |
| F | GLY359 | electrostatic stabiliser, hydrogen bond donor |
