Sandbox Reserved 431: Difference between revisions

Cytochrome P450 exists as an asymmetric dimer. Each dimeric unit contains 12 α-helices (labeled A-L) along with β-sheets, which are mostly located on one side of the molecule. Helices F and G form the dimeric interface of cytochrome P450, and are also involved in the formation of the active site. The dimeric interface of the protein is stabilized by electrostatic interactions between the <font color='red'>C terminus</font> of the G helix of one molecule (Arg259 and Asp255) with the <font color='blue'>N terminus</font> residues of the F helix of the second molecule (Asp206 and His209) and vice versa. Two molecules of 2-hydroxypropyl-β-cyclodextrin, which is used to dissolve vitamin D3, are also found near the dimer interface.