4FB2
Crystal Structure of Substrate-Free P450cin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046232 | biological_process | carbazole catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046232 | biological_process | carbazole catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046232 | biological_process | carbazole catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0055114 | biological_process | obsolete oxidation-reduction process |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046232 | biological_process | carbazole catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | ASN73 |
| A | THR243 |
| A | PRO284 |
| A | ARG289 |
| A | SER339 |
| A | LEU340 |
| A | GLY341 |
| A | ILE344 |
| A | HIS345 |
| A | CYS347 |
| A | ILE353 |
| A | MET90 |
| A | HOH605 |
| A | HOH616 |
| A | HOH730 |
| A | ALA91 |
| A | HIS98 |
| A | ARG102 |
| A | PHE109 |
| A | GLY238 |
| A | GLY239 |
| A | ASN242 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | ARG336 |
| A | HIS337 |
| A | GLY341 |
| A | HIS342 |
| A | HOH724 |
| A | HOH1066 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 503 |
| Chain | Residue |
| A | ARG122 |
| A | ARG358 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | ASN73 |
| B | MET90 |
| B | ALA91 |
| B | HIS98 |
| B | ARG102 |
| B | PHE109 |
| B | LEU235 |
| B | GLY238 |
| B | GLY239 |
| B | ASN242 |
| B | THR243 |
| B | ARG289 |
| B | SER339 |
| B | LEU340 |
| B | GLY341 |
| B | ILE344 |
| B | HIS345 |
| B | CYS347 |
| B | ILE353 |
| B | HOH601 |
| B | HOH658 |
| B | HOH750 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 502 |
| Chain | Residue |
| B | HIS337 |
| B | GLY341 |
| B | HIS342 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 503 |
| Chain | Residue |
| B | ARG122 |
| B | ARG358 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | ASN73 |
| C | MET90 |
| C | ALA91 |
| C | HIS98 |
| C | ARG102 |
| C | PHE109 |
| C | GLY238 |
| C | GLY239 |
| C | ASN242 |
| C | THR243 |
| C | PRO284 |
| C | VAL287 |
| C | ARG289 |
| C | SER339 |
| C | LEU340 |
| C | GLY341 |
| C | ILE344 |
| C | HIS345 |
| C | CYS347 |
| C | ILE353 |
| C | EDO505 |
| C | HOH603 |
| C | HOH658 |
| C | HOH670 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 502 |
| Chain | Residue |
| C | LEU264 |
| C | ILE265 |
| C | PRO268 |
| C | THR362 |
| C | HOH697 |
| C | HOH837 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 503 |
| Chain | Residue |
| C | ARG336 |
| C | HIS337 |
| C | GLY341 |
| C | HIS342 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 504 |
| Chain | Residue |
| C | ARG122 |
| C | ARG358 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO C 505 |
| Chain | Residue |
| C | HOH891 |
| C | HOH937 |
| C | HOH992 |
| C | ASN242 |
| C | ALA285 |
| C | HEM501 |
| C | HOH670 |
| C | HOH738 |
| C | HOH803 |
| site_id | BC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| D | ASN73 |
| D | MET90 |
| D | ALA91 |
| D | HIS98 |
| D | ARG102 |
| D | PHE109 |
| D | LEU235 |
| D | GLY238 |
| D | GLY239 |
| D | ASN242 |
| D | THR243 |
| D | PRO284 |
| D | VAL287 |
| D | ARG289 |
| D | SER339 |
| D | LEU340 |
| D | GLY341 |
| D | ILE344 |
| D | HIS345 |
| D | CYS347 |
| D | ILE353 |
| D | HOH607 |
| D | HOH653 |
| D | HOH1054 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 502 |
| Chain | Residue |
| D | ARG122 |
| D | ARG358 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15260491, ECO:0000269|PubMed:18270198, ECO:0000269|PubMed:22775403 |
| Chain | Residue | Details |
| A | ASN73 | |
| B | HIS345 | |
| C | ASN73 | |
| C | HIS98 | |
| C | ARG102 | |
| C | ARG289 | |
| C | HIS345 | |
| D | ASN73 | |
| D | HIS98 | |
| D | ARG102 | |
| D | ARG289 | |
| A | HIS98 | |
| D | HIS345 | |
| A | ARG102 | |
| A | ARG289 | |
| A | HIS345 | |
| B | ASN73 | |
| B | HIS98 | |
| B | ARG102 | |
| B | ARG289 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15260491 |
| Chain | Residue | Details |
| A | ASN242 | |
| B | ASN242 | |
| C | ASN242 | |
| D | ASN242 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS347 | |
| B | CYS347 | |
| C | CYS347 | |
| D | CYS347 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Controls regioselective substrate oxidation |
| Chain | Residue | Details |
| A | ASN242 | |
| B | ASN242 | |
| C | ASN242 | |
| D | ASN242 |
