4L6G
Crystal Structure of P450cin Y81F mutant, crystallized in 7 mM 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | ASN73 |
| A | THR243 |
| A | VAL287 |
| A | ARG289 |
| A | PHE312 |
| A | SER339 |
| A | LEU340 |
| A | GLY341 |
| A | ILE344 |
| A | HIS345 |
| A | CYS347 |
| A | VAL76 |
| A | ILE353 |
| A | HOH610 |
| A | MET90 |
| A | ALA91 |
| A | HIS98 |
| A | ARG102 |
| A | ILE234 |
| A | GLY238 |
| A | ASN242 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CNL A 502 |
| Chain | Residue |
| A | ASN242 |
| A | VAL386 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | ARG346 |
| A | ARG354 |
| A | HOH819 |
| A | HOH1044 |
| B | LYS69 |
| B | GLN293 |
| B | HOH620 |
| B | HOH687 |
| B | HOH917 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGE A 504 |
| Chain | Residue |
| A | TRP45 |
| A | GLY50 |
| A | LYS303 |
| A | PRO304 |
| A | GLY305 |
| A | GLN306 |
| A | HOH754 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | ASN73 |
| B | VAL76 |
| B | MET90 |
| B | ALA91 |
| B | HIS98 |
| B | ARG102 |
| B | ILE234 |
| B | LEU235 |
| B | GLY238 |
| B | ASN242 |
| B | THR243 |
| B | PHE246 |
| B | ARG289 |
| B | PHE312 |
| B | SER339 |
| B | LEU340 |
| B | GLY341 |
| B | ILE344 |
| B | HIS345 |
| B | CYS347 |
| B | LEU348 |
| B | ILE353 |
| B | CNL502 |
| B | HOH610 |
| B | HOH813 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CNL B 502 |
| Chain | Residue |
| B | ASN242 |
| B | VAL386 |
| B | HEM501 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | ARG346 |
| B | ALA350 |
| B | ARG354 |
| B | HOH835 |
| B | HOH959 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| A | ASN207 |
| A | HOH784 |
| B | ARG122 |
| B | ARG358 |
| B | HOH774 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE B 505 |
| Chain | Residue |
| B | TRP45 |
| B | GLY50 |
| B | PRO304 |
| B | GLY305 |
| B | HOH699 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15260491","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18270198","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22775403","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15260491","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Controls regioselective substrate oxidation"} |
| Chain | Residue | Details |
