3TMZ
Crystal Structure of P450 2B4(H226Y) in complex with Amlodipine
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 | arachidonic acid 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 |
| A | 0070330 | molecular_function | aromatase activity |
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 | THR306 |
| A | VAL367 |
| A | HIS369 |
| A | PRO428 |
| A | PHE429 |
| A | SER430 |
| A | ARG434 |
| A | CYS436 |
| A | LEU437 |
| A | GLY438 |
| A | VAL113 |
| A | 06X503 |
| A | HOH684 |
| A | ILE114 |
| A | TRP121 |
| A | ARG125 |
| A | ALA298 |
| A | GLY299 |
| A | THR302 |
| A | THR303 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CM5 A 502 |
| Chain | Residue |
| A | PHE184 |
| A | LYS186 |
| A | PHE188 |
| A | VAL194 |
| A | PHE195 |
| A | PHE244 |
| A | LYS251 |
| A | HOH631 |
| A | HOH638 |
| A | HOH734 |
| A | HOH770 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 06X A 503 |
| Chain | Residue |
| A | ILE101 |
| A | ILE114 |
| A | PHE115 |
| A | PHE206 |
| A | ILE209 |
| A | PHE297 |
| A | ALA298 |
| A | GLU301 |
| A | THR302 |
| A | VAL367 |
| A | VAL477 |
| A | HEM501 |
| A | 06X504 |
| A | HOH705 |
| A | HOH790 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 06X A 504 |
| Chain | Residue |
| A | LEU51 |
| A | LEU70 |
| A | ILE101 |
| A | ILE209 |
| A | GLN215 |
| A | GLU218 |
| A | PHE365 |
| A | GLU387 |
| A | VAL477 |
| A | 06X503 |
| A | HOH794 |
| A | HOH795 |
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 | GLN455 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P00176 |
| Chain | Residue | Details |
| A | GLN147 |
