4FMX
Crystal Structure of Substrate-Bound 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM A 501 |
Chain | Residue |
A | ASN73 |
A | ASN242 |
A | THR243 |
A | ARG289 |
A | PHE312 |
A | SER339 |
A | LEU340 |
A | GLY341 |
A | ILE344 |
A | HIS345 |
A | CYS347 |
A | VAL76 |
A | ILE353 |
A | CNL502 |
A | HOH630 |
A | HOH959 |
A | MET90 |
A | ALA91 |
A | HIS98 |
A | ARG102 |
A | PHE109 |
A | ILE234 |
A | GLY238 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CNL A 502 |
Chain | Residue |
A | ASN242 |
A | VAL386 |
A | HEM501 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | ARG346 |
A | ALA350 |
A | HIS351 |
A | ARG354 |
A | HOH821 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 504 |
Chain | Residue |
A | ARG253 |
A | ASP257 |
A | GLU259 |
A | ARG263 |
A | ILE328 |
A | GOL505 |
A | HOH615 |
A | HOH649 |
B | ARG253 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 505 |
Chain | Residue |
A | ARG253 |
A | ASN327 |
A | GOL504 |
B | ARG253 |
B | ASP257 |
B | GLU259 |
B | ARG263 |
B | ILE328 |
B | HOH619 |
B | HOH630 |
site_id | AC6 |
Number of Residues | 22 |
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 | GLY238 |
B | ASN242 |
B | THR243 |
B | ARG289 |
B | PHE312 |
B | SER339 |
B | LEU340 |
B | GLY341 |
B | ILE344 |
B | HIS345 |
B | CYS347 |
B | LEU348 |
B | ILE353 |
B | CNL502 |
B | HOH663 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CNL B 502 |
Chain | Residue |
B | ASN242 |
B | VAL287 |
B | HEM501 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 503 |
Chain | Residue |
B | ARG346 |
B | ALA350 |
B | HIS351 |
B | ARG354 |
B | HOH806 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 504 |
Chain | Residue |
B | PRO272 |
B | ARG354 |
B | ARG358 |
B | HOH918 |
B | HOH950 |
B | HOH956 |
B | HOH988 |
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 | |
B | HIS345 | |
A | HIS98 | |
A | ARG102 | |
A | ARG289 | |
A | HIS345 | |
B | ASN73 | |
B | HIS98 | |
B | ARG102 | |
B | ARG289 |
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 |