5FYF
Structure of CYP153A from Marinobacter aquaeolei
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 | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0020037 | molecular_function | heme binding |
A | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
A | 0046872 | molecular_function | metal ion binding |
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 | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0020037 | molecular_function | heme binding |
B | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 1475 |
Chain | Residue |
B | ASP122 |
B | THR316 |
B | SER319 |
B | MET361 |
B | ARG363 |
B | TYR386 |
B | SER414 |
B | PHE415 |
B | GLY416 |
B | TYR417 |
B | VAL419 |
B | PHE148 |
B | HIS420 |
B | CYS422 |
B | GLY424 |
B | ALA428 |
B | ILE149 |
B | HIS156 |
B | ARG160 |
B | LEU214 |
B | GLY311 |
B | GLY312 |
B | THR315 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM A 1475 |
Chain | Residue |
A | ASP122 |
A | PHE148 |
A | ILE149 |
A | HIS156 |
A | ARG160 |
A | LEU214 |
A | GLY311 |
A | GLY312 |
A | THR315 |
A | THR316 |
A | SER319 |
A | MET361 |
A | ARG363 |
A | TYR386 |
A | SER414 |
A | PHE415 |
A | GLY416 |
A | TYR417 |
A | VAL419 |
A | HIS420 |
A | CYS422 |
A | GLY424 |
A | LEU427 |
A | ALA428 |
A | HOH2075 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 1476 |
Chain | Residue |
A | VAL121 |
A | ASP122 |
A | SER124 |
A | HIS125 |
A | PHE128 |
A | ARG363 |
A | HIS420 |
A | HOH2063 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1477 |
Chain | Residue |
A | ARG461 |
A | HOH2022 |
A | HOH2023 |
A | HOH2181 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1476 |
Chain | Residue |
B | TRP385 |
B | ARG461 |
B | HOH2002 |
B | HOH2003 |
B | HOH2099 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGyGVHRCMG |
Chain | Residue | Details |
A | PHE415-GLY424 |