Sandbox Reserved 1709: Difference between revisions

Within the four transmembrane helices lies the <scene name='90/904314/Binding_pocket/1'>binding pocket</scene>. The binding pocket holds <scene name='90/904314/Active_site/3'>two hydrophilic residues</scene> active site residues, N80 and Y139, that interact with the substrate. N80 and Y139 are surrounded by a <scene name='90/906893/Hydrophobic/3'>hydrophobic region</scene> that provides specificity to the region. The hydrophilic residues hydrogen bond to the substrate, providing recognition and increasing specificity. The <scene name='90/906893/Disulfide_-_132/1'>C132-C135 disulfide bridge</scene> above the binding pocket provides stabilization when a substrate is bound. This bridge provides increased stability for the binding site as it interacts with and binds substrates or inhibitors. The hydrophilic residues provide <scene name='90/906893/K_hbonds/1'>hydrogen bonds</scene> when interacting with substrates for specificity and recognition. Upon binding, VKOR will transition into the closed conformation allowing the catalytic mechanism to commence.