3KW4
Crystal structure of cytochrome 2B4 in complex with the anti-platelet drug ticlopidine
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 | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 500 |
Chain | Residue |
A | ARG98 |
A | ILE363 |
A | HIS369 |
A | PRO428 |
A | PHE429 |
A | SER430 |
A | ARG434 |
A | CYS436 |
A | LEU437 |
A | GLY438 |
A | TIC600 |
A | ILE114 |
A | TRP121 |
A | ARG125 |
A | ALA298 |
A | GLY299 |
A | THR302 |
A | THR303 |
A | THR306 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TIC A 600 |
Chain | Residue |
A | ILE114 |
A | PHE206 |
A | ILE209 |
A | SER210 |
A | PHE297 |
A | ALA298 |
A | GLU301 |
A | THR302 |
A | VAL367 |
A | GLY478 |
A | HEM500 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CM5 A 601 |
Chain | Residue |
A | LEU43 |
A | MET46 |
A | ASP47 |
A | LEU219 |
A | TYR226 |
A | PHE227 |
A | HOH1028 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CM5 A 602 |
Chain | Residue |
A | LYS186 |
A | PHE188 |
A | PHE195 |
A | LEU198 |
A | PHE202 |
A | ILE241 |
A | PHE244 |
A | LYS251 |
A | PHE296 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CH0 A 603 |
Chain | Residue |
A | PHE212 |
A | PHE227 |
A | GLU474 |
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 |