1T2B
Crystal Structure of cytochrome P450cin complexed with its substrate 1,8-cineole
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 450 |
| Chain | Residue |
| A | ASN73 |
| A | ASN242 |
| A | THR243 |
| A | PRO284 |
| A | ARG289 |
| A | PHE312 |
| A | SER339 |
| A | LEU340 |
| A | GLY341 |
| A | ILE344 |
| A | HIS345 |
| A | VAL76 |
| A | CYS347 |
| A | LEU348 |
| A | ILE353 |
| A | CNL500 |
| A | HOH528 |
| A | MET90 |
| A | ALA91 |
| A | HIS98 |
| A | ARG102 |
| A | PHE109 |
| A | ILE234 |
| A | GLY238 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CNL A 500 |
| Chain | Residue |
| A | THR77 |
| A | GLY238 |
| A | ASN242 |
| A | VAL287 |
| A | VAL386 |
| A | HEM450 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM B 450 |
| Chain | Residue |
| B | ASN73 |
| B | VAL76 |
| B | MET90 |
| B | ALA91 |
| B | HIS98 |
| B | ARG102 |
| B | PHE109 |
| B | ILE234 |
| B | GLY238 |
| B | ASN242 |
| B | THR243 |
| B | PRO284 |
| B | ARG289 |
| B | PHE312 |
| B | SER339 |
| B | LEU340 |
| B | GLY341 |
| B | ILE344 |
| B | HIS345 |
| B | CYS347 |
| B | ILE353 |
| B | CNL500 |
| B | HOH513 |
| B | HOH850 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CNL B 500 |
| Chain | Residue |
| B | THR77 |
| B | GLY238 |
| B | ASN242 |
| B | ALA285 |
| B | VAL287 |
| B | VAL386 |
| B | HEM450 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15260491, ECO:0000269|PubMed:18270198, ECO:0000269|PubMed:22775403 |
| Chain | Residue | Details |
| A | ASN73 | |
| A | HIS98 | |
| A | ARG102 | |
| A | ARG289 | |
| A | HIS345 | |
| B | ASN73 | |
| B | HIS98 | |
| B | ARG102 | |
| B | ARG289 | |
| B | HIS345 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15260491 |
| Chain | Residue | Details |
| A | ASN242 | |
| B | ASN242 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS347 | |
| B | CYS347 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Controls regioselective substrate oxidation |
| Chain | Residue | Details |
| A | ASN242 | |
| B | ASN242 |
