4DO1
The crystal structures of 4-methoxybenzoate bound 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 | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | ILE97 |
| A | PHE298 |
| A | ARG300 |
| A | GLY350 |
| A | PHE351 |
| A | GLY352 |
| A | HIS356 |
| A | CYS358 |
| A | VAL359 |
| A | GLY360 |
| A | ALA364 |
| A | LEU98 |
| A | ANN502 |
| A | HOH637 |
| A | HOH643 |
| A | HIS105 |
| A | ARG109 |
| A | PHE160 |
| A | ALA248 |
| A | GLY249 |
| A | THR252 |
| A | THR253 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ANN A 502 |
| Chain | Residue |
| A | ARG92 |
| A | SER95 |
| A | ILE97 |
| A | PHE182 |
| A | SER244 |
| A | SER247 |
| A | ALA248 |
| A | PHE298 |
| A | HEM501 |
| A | HOH645 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | ARG109 |
| A | SER113 |
| A | GOL504 |
| A | HOH652 |
| A | HOH817 |
| A | HOH952 |
| A | HOH1016 |
| C | LYS114 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 504 |
| Chain | Residue |
| A | SER113 |
| A | LEU116 |
| A | SER117 |
| A | VAL359 |
| A | GLN361 |
| A | LEU362 |
| A | SO4503 |
| A | HOH1091 |
| A | HOH1123 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 505 |
| Chain | Residue |
| A | ARG92 |
| A | TYR177 |
| A | GLN203 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | ILE97 |
| B | LEU98 |
| B | HIS105 |
| B | ARG109 |
| B | ALA248 |
| B | GLY249 |
| B | THR252 |
| B | THR253 |
| B | VAL295 |
| B | PHE298 |
| B | ARG300 |
| B | GLY350 |
| B | PHE351 |
| B | GLY352 |
| B | HIS356 |
| B | CYS358 |
| B | VAL359 |
| B | GLY360 |
| B | ALA364 |
| B | ANN502 |
| B | HOH661 |
| B | HOH1041 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ANN B 502 |
| Chain | Residue |
| B | ARG92 |
| B | SER95 |
| B | ILE97 |
| B | PHE182 |
| B | SER244 |
| B | SER247 |
| B | ALA248 |
| B | PHE298 |
| B | HEM501 |
| B | HOH643 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | ARG109 |
| B | SER113 |
| B | GOL505 |
| B | HOH638 |
| B | HOH789 |
| B | HOH853 |
| D | LYS114 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| B | ARG78 |
| B | LYS86 |
| B | LYS87 |
| B | GLY316 |
| B | HOH1057 |
| B | HOH1067 |
| D | THR40 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 505 |
| Chain | Residue |
| B | LEU116 |
| B | SER117 |
| B | VAL359 |
| B | GLN361 |
| B | LEU362 |
| B | SO4503 |
| B | HOH835 |
| B | HOH947 |
| B | SER113 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 506 |
| Chain | Residue |
| B | ARG92 |
| B | TYR177 |
| B | GLN203 |
| B | HOH709 |
| site_id | BC3 |
| Number of Residues | 24 |
| 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 | LEU323 |
| C | GLY350 |
| C | PHE351 |
| C | GLY352 |
| C | HIS356 |
| C | CYS358 |
| C | VAL359 |
| C | GLY360 |
| C | ALA364 |
| C | ANN502 |
| C | HOH627 |
| C | HOH629 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ANN C 502 |
| Chain | Residue |
| C | ARG92 |
| C | SER95 |
| C | LEU98 |
| C | PHE182 |
| C | SER244 |
| C | SER247 |
| C | ALA248 |
| C | PHE298 |
| C | HEM501 |
| C | HOH1013 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 C 503 |
| Chain | Residue |
| A | LYS114 |
| A | HOH976 |
| C | ARG109 |
| C | SER113 |
| C | GOL504 |
| C | HOH648 |
| C | HOH744 |
| C | HOH1144 |
| C | HOH1149 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 504 |
| Chain | Residue |
| C | SER113 |
| C | LEU116 |
| C | SER117 |
| C | VAL359 |
| C | GLN361 |
| C | LEU362 |
| C | SO4503 |
| C | HOH1130 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 505 |
| Chain | Residue |
| C | ARG92 |
| C | TYR177 |
| C | GLN203 |
| site_id | BC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| D | ILE97 |
| D | LEU98 |
| D | HIS105 |
| D | ARG109 |
| D | PHE160 |
| D | ALA248 |
| D | GLY249 |
| D | THR252 |
| D | THR253 |
| D | VAL295 |
| D | PHE298 |
| D | ARG300 |
| D | LEU323 |
| D | GLY350 |
| D | PHE351 |
| D | GLY352 |
| D | HIS356 |
| D | CYS358 |
| D | VAL359 |
| D | GLY360 |
| D | ALA364 |
| D | ANN502 |
| D | HOH632 |
| D | HOH636 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ANN D 502 |
| Chain | Residue |
| D | ARG92 |
| D | SER95 |
| D | LEU98 |
| D | PHE182 |
| D | SER244 |
| D | SER247 |
| D | ALA248 |
| D | PHE298 |
| D | HEM501 |
| D | HOH1014 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 503 |
| Chain | Residue |
| B | LYS114 |
| D | ARG109 |
| D | SER113 |
| D | GOL504 |
| D | HOH644 |
| D | HOH843 |
| D | HOH1079 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 504 |
| Chain | Residue |
| D | SER113 |
| D | LEU116 |
| D | SER117 |
| D | VAL359 |
| D | GLN361 |
| D | SO4503 |
| D | HOH818 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 505 |
| Chain | Residue |
| D | ARG92 |
| 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 |
