4DNZ
The crystal structures of CYP199A4
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 | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| 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 | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | ILE97 |
| A | ARG300 |
| A | GLY350 |
| A | PHE351 |
| A | GLY352 |
| A | HIS356 |
| A | CYS358 |
| A | GLY360 |
| A | HOH632 |
| A | LEU98 |
| A | HIS105 |
| A | ARG109 |
| A | ALA248 |
| A | GLY249 |
| A | THR252 |
| A | THR253 |
| A | PHE298 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ARG109 |
| A | GOL503 |
| A | HOH676 |
| D | LYS114 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | SER113 |
| A | VAL359 |
| A | GLN361 |
| A | SO4502 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 504 |
| Chain | Residue |
| A | TYR177 |
| A | GLN203 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | ILE97 |
| B | LEU98 |
| B | HIS105 |
| B | ARG109 |
| B | PHE160 |
| B | ALA248 |
| B | GLY249 |
| B | THR252 |
| B | THR253 |
| B | PHE298 |
| B | ARG300 |
| B | GLY350 |
| B | PHE351 |
| B | GLY352 |
| B | HIS356 |
| B | CYS358 |
| B | GLY360 |
| B | HOH671 |
| B | HOH704 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| B | ARG109 |
| B | GOL503 |
| B | HOH611 |
| C | LYS114 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | SER113 |
| B | LEU116 |
| B | SER117 |
| B | GLN361 |
| B | LEU362 |
| B | SO4502 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 504 |
| Chain | Residue |
| B | TYR177 |
| B | GLN203 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | ILE97 |
| C | LEU98 |
| C | HIS105 |
| C | ARG109 |
| C | PHE160 |
| C | ALA248 |
| C | GLY249 |
| C | THR252 |
| C | THR253 |
| C | VAL295 |
| C | PHE298 |
| C | ARG300 |
| C | GLY350 |
| C | PHE351 |
| C | GLY352 |
| C | HIS356 |
| C | CYS358 |
| C | VAL359 |
| C | GLY360 |
| C | HOH648 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 502 |
| Chain | Residue |
| B | LYS114 |
| C | ARG109 |
| C | SER113 |
| C | GOL503 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 503 |
| Chain | Residue |
| C | SER113 |
| C | LEU116 |
| C | SER117 |
| C | GLN361 |
| C | LEU362 |
| C | SO4502 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 504 |
| Chain | Residue |
| C | ARG92 |
| C | TYR177 |
| C | GLN203 |
| C | ARG243 |
| site_id | BC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| D | GLY249 |
| D | THR252 |
| D | THR253 |
| D | VAL295 |
| D | PHE298 |
| D | ARG300 |
| D | GLY350 |
| D | PHE351 |
| D | VAL355 |
| D | HIS356 |
| D | CYS358 |
| D | VAL359 |
| D | GLY360 |
| D | ALA364 |
| D | HOH613 |
| D | LEU68 |
| D | ILE97 |
| D | LEU98 |
| D | HIS105 |
| D | ARG109 |
| D | LEU245 |
| D | ALA248 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 502 |
| Chain | Residue |
| A | LYS114 |
| D | ARG109 |
| D | SER113 |
| D | GOL503 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 503 |
| Chain | Residue |
| D | SER113 |
| D | LEU116 |
| D | SER117 |
| D | VAL359 |
| D | GLN361 |
| D | SO4502 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 504 |
| Chain | Residue |
| D | TYR177 |
| D | GLN203 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGVHMCVG |
| Chain | Residue | Details |
| A | PHE351-GLY360 |
