Sandbox Reserved 1716: Difference between revisions
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== Structure == | == Structure == | ||
The VKOR enzyme is made up of four transmembrane helices: | The VKOR enzyme is made up of four transmembrane helices: <scene name='90/904321/Tm1/1'>TM1</scene>, <scene name='90/904321/Tm2/1'>TM2</scene>, <scene name='90/904321/Tm3/1'>TM3</scene>, and <scene name='90/904321/Tm4/1'>TM4</scene> .(Grey/Orange) Each of these helices come together to form a central ligand binding pocket. This central pocket is the active site where conserved Cysteines: C132 and C135 are located. In the cap domain are important regions that are significant for Vitamin K binding, and the overall function of Vitamin K Epoxide Reductase, including the Anchor(Green), Cap Sequence (Blue), Beta Hairpin (Purple), and 3-4 Loop (Pink). | ||
The <scene name='90/904321/Anchor/3'>Anchor</scene> attaches to the cap domain of the Vitamin K Epoxide Reductase Enzyme and is partially embedded in the Endoplasmic Reticulum Membrane. This both stabilizes the enzyme in the membrane, and stabilizes the cap domain over the active site. | The <scene name='90/904321/Anchor/3'>Anchor</scene> attaches to the cap domain of the Vitamin K Epoxide Reductase Enzyme and is partially embedded in the Endoplasmic Reticulum Membrane. This both stabilizes the enzyme in the membrane, and stabilizes the cap domain over the active site. | ||
