5UEC
Crystal Structure of CYP2B6 (Y226H/K262R) in complex with myrtenyl bromide.
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 | 0006629 | biological_process | lipid metabolic process |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0008202 | biological_process | steroid metabolic process |
A | 0008390 | molecular_function | testosterone 16-alpha-hydroxylase activity |
A | 0008392 | molecular_function | arachidonate epoxygenase activity |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
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 | 0042178 | biological_process | xenobiotic catabolic process |
A | 0042180 | biological_process | ketone metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0062184 | molecular_function | testosterone 16-beta-hydroxylase activity |
A | 0062187 | molecular_function | anandamide 8,9 epoxidase activity |
A | 0062188 | molecular_function | anandamide 11,12 epoxidase activity |
A | 0062189 | molecular_function | anandamide 14,15 epoxidase activity |
A | 0101021 | molecular_function | estrogen 2-hydroxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | ARG98 |
A | VAL367 |
A | HIS369 |
A | PRO428 |
A | PHE429 |
A | SER430 |
A | ARG434 |
A | CYS436 |
A | LEU437 |
A | GLY438 |
A | 85D505 |
A | TRP121 |
A | ARG125 |
A | ILE179 |
A | GLY299 |
A | THR302 |
A | THR306 |
A | LEU362 |
A | LEU363 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CM5 A 502 |
Chain | Residue |
A | PHE188 |
A | GLU194 |
A | MET198 |
A | TYR244 |
A | PHE296 |
A | LYS384 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue CM5 A 503 |
Chain | Residue |
A | PHE223 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CM5 A 504 |
Chain | Residue |
A | LEU43 |
A | MET46 |
A | ARG48 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue 85D A 505 |
Chain | Residue |
A | ILE114 |
A | PHE297 |
A | ALA298 |
A | THR302 |
A | LEU363 |
A | HEM501 |
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 | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | CYS436 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000250 |
Chain | Residue | Details |
A | SER128 |