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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
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 | VAL359 |
A | GLY360 |
A | ALA364 |
A | FIV502 |
A | LEU98 |
A | HIS105 |
A | ARG109 |
A | LEU116 |
A | ALA248 |
A | GLY249 |
A | THR252 |
A | PHE298 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE FIV A 502 |
Chain | Residue |
A | ARG92 |
A | SER95 |
A | LEU98 |
A | VAL181 |
A | PHE182 |
A | ARG243 |
A | SER244 |
A | SER247 |
A | ALA248 |
A | HEM501 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FIV A 503 |
Chain | Residue |
A | GLY179 |
A | ASN183 |
A | ALA195 |
A | ASP251 |
A | ARG391 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | ARG107 |
A | HOH607 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 505 |
Chain | Residue |
A | ARG109 |
A | SER113 |
A | GOL506 |
B | LYS114 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 506 |
Chain | Residue |
A | SER113 |
A | SER117 |
A | GLN361 |
A | LEU362 |
A | SO4505 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 507 |
Chain | Residue |
A | ARG92 |
A | TYR177 |
A | GLN203 |
A | ARG243 |
site_id | AC8 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM B 501 |
Chain | Residue |
B | ILE97 |
B | LEU98 |
B | HIS105 |
B | ARG109 |
B | LEU245 |
B | ALA248 |
B | GLY249 |
B | THR252 |
B | THR253 |
B | VAL295 |
B | ARG300 |
B | PHE351 |
B | HIS356 |
B | CYS358 |
B | VAL359 |
B | GLY360 |
B | FIV502 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FIV B 502 |
Chain | Residue |
B | ARG92 |
B | SER95 |
B | LEU98 |
B | VAL181 |
B | PHE182 |
B | LEU240 |
B | SER244 |
B | ALA248 |
B | HEM501 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 503 |
Chain | Residue |
A | LYS114 |
B | ARG109 |
B | SER113 |
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 | |