Sandbox Reserved 1724: Difference between revisions

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=== Active Site ===

VKOR uses two catalytic amino acids, ~~tyrosine 139 and asparagine 80, to stabilize binding to all forms of~~ <scene name='90/904329/Kohhbond/2'>~~vitamin K~~</scene> and <scene name='90/904329/Warfarinhbond/3'>vitamin K antagonists</scene>, such as Warfarin, in the binding pocket. Tyr139 and Asn80 hydrogen bond to carbonyl groups on both structures and stabilizes them within the binding pocket <ref name="Liu">PMID:33154105</ref>.

VKOR uses two catalytic amino acids, <scene name='90/904329/Kohhbond/3'>tyrosine 139 and asparagine 80</scene>, to stabilize binding to all forms of vitamin K and <scene name='90/904329/Warfarinhbond/3'>vitamin K antagonists</scene>, such as Warfarin, in the binding pocket. Tyr139 and Asn80 hydrogen bond to carbonyl groups on both structures and stabilizes them within the binding pocket <ref name="Liu">PMID:33154105</ref>.

Other than the two previously mentioned hydrogen bonds (Tyr139 and Asn80), <scene name='90/904329/Kohhydrophobic/2'>vitamin K</scene> and <scene name='90/904329/Warfarinhydrophobic/1'> VKOR antagonists</scene> are bound via hydrophobic interactions within the binding pocket of VKOR. Hydrophobic residues of VKOR such as Phe80, Phe87, and Tyr88, form a hydrophobic tunnel within the binding pocket <ref name="Liu">PMID:33154105</ref>.

Sandbox Reserved 1724: Difference between revisions

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@@ Line 16: / Line 16: @@
 === Active Site ===
-VKOR uses two catalytic amino acids, tyrosine 139 and asparagine 80, to stabilize binding to all forms of <scene name='90/904329/Kohhbond/2'>vitamin K</scene> and <scene name='90/904329/Warfarinhbond/3'>vitamin K antagonists</scene>, such as Warfarin, in the binding pocket. Tyr139 and Asn80 hydrogen bond to carbonyl groups on both structures and stabilizes them within the binding pocket <ref name="Liu">PMID:33154105</ref>.
+VKOR uses two catalytic amino acids, <scene name='90/904329/Kohhbond/3'>tyrosine 139 and asparagine 80</scene>, to stabilize binding to all forms of vitamin K and <scene name='90/904329/Warfarinhbond/3'>vitamin K antagonists</scene>, such as Warfarin, in the binding pocket. Tyr139 and Asn80 hydrogen bond to carbonyl groups on both structures and stabilizes them within the binding pocket <ref name="Liu">PMID:33154105</ref>.
 Other than the two previously mentioned hydrogen bonds (Tyr139 and Asn80), <scene name='90/904329/Kohhydrophobic/2'>vitamin K</scene> and <scene name='90/904329/Warfarinhydrophobic/1'> VKOR antagonists</scene> are bound via hydrophobic interactions within the binding pocket of VKOR. Hydrophobic residues of VKOR such as Phe80, Phe87, and Tyr88, form a hydrophobic tunnel within the binding pocket <ref name="Liu">PMID:33154105</ref>.