5IUZ
STRUCTURE OF P450 2B4 F202W MUTANT (CYMAL-5)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0008392 | molecular_function | arachidonate epoxygenase activity |
A | 0016020 | cellular_component | membrane |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
A | 0019373 | biological_process | epoxygenase P450 pathway |
A | 0020037 | molecular_function | heme binding |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0046872 | molecular_function | metal ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0006805 | biological_process | xenobiotic metabolic process |
B | 0008392 | molecular_function | arachidonate epoxygenase activity |
B | 0016020 | cellular_component | membrane |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
B | 0019373 | biological_process | epoxygenase P450 pathway |
B | 0020037 | molecular_function | heme binding |
B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | ARG98 |
A | THR303 |
A | THR306 |
A | VAL367 |
A | HIS369 |
A | LEU392 |
A | PRO428 |
A | SER430 |
A | ARG434 |
A | CYS436 |
A | LEU437 |
A | VAL113 |
A | GLY438 |
A | ALA442 |
A | ILE114 |
A | TRP121 |
A | ARG125 |
A | ILE179 |
A | ALA298 |
A | GLY299 |
A | THR302 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CM5 A 502 |
Chain | Residue |
A | LYS186 |
A | PHE188 |
A | LEU198 |
A | PHE244 |
A | LYS251 |
A | ASP467 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue CM5 A 503 |
Chain | Residue |
A | LEU44 |
A | MET46 |
A | ASP47 |
A | GLY50 |
A | VAL216 |
A | HOH648 |
A | HOH679 |
A | HOH721 |
site_id | AC4 |
Number of Residues | 20 |
Details | binding site for residue HEM B 501 |
Chain | Residue |
B | ARG98 |
B | ILE114 |
B | TRP121 |
B | ARG125 |
B | ALA298 |
B | GLY299 |
B | THR302 |
B | THR303 |
B | THR306 |
B | ILE363 |
B | VAL367 |
B | HIS369 |
B | LEU392 |
B | PRO428 |
B | SER430 |
B | ARG434 |
B | CYS436 |
B | LEU437 |
B | GLY438 |
B | HOH636 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue CM5 B 502 |
Chain | Residue |
B | PHE188 |
B | PHE195 |
B | LEU198 |
B | PHE244 |
B | PHE296 |
B | ASP467 |
B | HOH601 |
B | HOH668 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CM5 B 503 |
Chain | Residue |
B | LEU43 |
B | MET46 |
B | ASP47 |
B | GLY50 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSlGKRICLG |
Chain | Residue | Details |
A | PHE429-GLY438 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | GLN455 | |
B | GLN455 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P00176 |
Chain | Residue | Details |
A | GLN147 | |
B | GLN147 |