2BVJ
Ligand-free structure of cytochrome P450 PikC (CYP107L1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0020037 | molecular_function | heme binding |
| A | 0033068 | biological_process | macrolide biosynthetic process |
| A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| 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 | 0006707 | biological_process | cholesterol catabolic process |
| B | 0008395 | molecular_function | steroid hydroxylase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| B | 0033068 | biological_process | macrolide biosynthetic process |
| B | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| 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 | 26 |
| Details | BINDING SITE FOR RESIDUE HEM A1408 |
| Chain | Residue |
| A | LYS72 |
| A | THR248 |
| A | LEU251 |
| A | PRO289 |
| A | ALA293 |
| A | THR294 |
| A | ARG296 |
| A | ALA346 |
| A | PHE347 |
| A | GLY348 |
| A | ILE351 |
| A | MET92 |
| A | HIS352 |
| A | CYS354 |
| A | ILE355 |
| A | GLY356 |
| A | ALA360 |
| A | HOH2087 |
| A | HOH2144 |
| A | LEU93 |
| A | HIS100 |
| A | ARG104 |
| A | PHE111 |
| A | ALA243 |
| A | GLY244 |
| A | THR247 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME A1409 |
| Chain | Residue |
| A | LEU135 |
| A | ARG374 |
| A | CYS375 |
| A | TRP405 |
| A | HOH2143 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DTT A1410 |
| Chain | Residue |
| A | ARG120 |
| A | ASP277 |
| A | ARG365 |
| A | ARG369 |
| A | HOH2098 |
| B | GLY21 |
| B | GLN22 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM B1408 |
| Chain | Residue |
| B | LYS72 |
| B | MET92 |
| B | LEU93 |
| B | HIS100 |
| B | ARG104 |
| B | PHE111 |
| B | LEU240 |
| B | ALA243 |
| B | GLY244 |
| B | THR247 |
| B | THR248 |
| B | LEU251 |
| B | ALA293 |
| B | THR294 |
| B | ARG296 |
| B | ALA346 |
| B | PHE347 |
| B | GLY348 |
| B | HIS352 |
| B | CYS354 |
| B | ILE355 |
| B | ALA360 |
| B | HOH2101 |
| B | HOH2140 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME B1409 |
| Chain | Residue |
| B | LEU135 |
| B | ARG374 |
| B | CYS375 |
| B | TRP405 |
| B | HOH2168 |
| B | HOH2169 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCIG |
| Chain | Residue | Details |
| A | PHE347-GLY356 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459 |
| Chain | Residue | Details |
| A | GLU94 | |
| A | ALA187 | |
| A | HIS238 | |
| B | GLU94 | |
| B | ALA187 | |
| B | HIS238 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000312|PDB:2C6H, ECO:0000312|PDB:2C7X, ECO:0000312|PDB:2CA0, ECO:0000312|PDB:2CD8, ECO:0000312|PDB:2VZ7, ECO:0000312|PDB:2VZM, ECO:0000312|PDB:2WHW, ECO:0000312|PDB:2WI9, ECO:0000312|PDB:3ZK5, ECO:0000312|PDB:4B7D, ECO:0000312|PDB:4B7S, ECO:0000312|PDB:4BF4 |
| Chain | Residue | Details |
| A | CYS354 | |
| B | CYS354 |
