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 | 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 | 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 | 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 | 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 |