Sandbox Reserved 1709: Difference between revisions
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== Structural Highlights== | == Structural Highlights== | ||
=== Active Site === | === Active Site === | ||
Within the four transmembrane helices lies the active site. The active site is comprised of a hydrophobic pocket containing two hydrophilic residues, A80 and Y139, that interact with substrates and ligands alike. The hydrophobic pocket provides specificity to the region while the hydrophilic residues have potential to hydrogen bond, allowing recognition and increasing specificity as well. Slightly above the active site is a crucial disulfide bridge that provides stabilization when a substrate is bound. This bridge occurs between C132 and C135, recurrent residues that continually aid in VKOR function. | |||
The <scene name='90/906893/Active_site/2'>active site</scene> plays a vital role in binding of any substrate or ligand to the VKOR. Upon binding, the VKOR will transition into a <scene name='90/906893/Closed_conformation/4'>closed conformation</scene> that will allow its catalytic mechanism to commence. | The <scene name='90/906893/Active_site/2'>active site</scene> plays a vital role in binding of any substrate or ligand to the VKOR. Upon binding, the VKOR will transition into a <scene name='90/906893/Closed_conformation/4'>closed conformation</scene> that will allow its catalytic mechanism to commence. | ||
