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<scene name='90/904321/Closedconformation/2'>Spinning VKOR</scene>
<scene name='90/904321/Closedconformation/2'>Spinning VKOR</scene>
[https://en.wikipedia.org/wiki/Vitamin_K_epoxide_reductase VKOR WIKI]
[https://en.wikipedia.org/wiki/Vitamin_K_epoxide_reductase VKOR WIKI]
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. <ref name="Ransey">PMID:28504306</ref>
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The VKOR enzyme is made up of four transmembrane helices: T1, T2, T3, and T4.(Pictured in Grey) Each of these helices come together to form a hydrophobic pocket, that is topped by a cap domain. In the cap domain are important regions that are significant for Vitamin K binding, and the overall function of Vitamin K Epoxide Reductase. These important regions are the Anchor(Green), Cap Region (Blue), Beta Hairpin (Purple), and 3-4 Loop (Pink).
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<ref name="Ransey">PMID:28504306</ref>
===Transmembrane Helices===
===Transmembrane Helices===
===Cap Domain===
===Cap Domain===

Revision as of 15:42, 24 March 2022

Vitamin K Epoxide Reductase

Structure of Closed Vitamin K Epoxide Reductase (PDB entry 6wv3)

Drag the structure with the mouse to rotate

References

  1. Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677
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