Sandbox Reserved 1709: Difference between revisions

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=== Active Site ===

Within the four transmembrane helices lies the <scene name='90/906893/Binding_pocket/1'>binding pocket</scene>. The binding pocket is comprised of a <scene name='90/906893/Hydrophobic/2'>hydrophobic region</scene> containing <scene name='90/906893/Active_site/7'>two hydrophilic residues</scene>, N80 and Y139, that interact with substrates. The hydrophobic pocket provides specificity to the region while 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.

Within the four transmembrane helices lies the <scene name='90/906893/Binding_pocket/1'>binding pocket</scene>. The binding pocket is comprised of a <scene name='90/906893/Hydrophobic/2'>hydrophobic region</scene> containing <scene name='90/906893/Active_site/7'>two hydrophilic residues</scene>, N80 and Y139, that interact with substrates. The hydrophobic pocket provides specificity to the region while 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='90/904314/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.

==Catalytic Mechanism of VKOR==

Sandbox Reserved 1709: Difference between revisions

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@@ Line 20: / Line 20: @@
 === Active Site ===
-Within the four transmembrane helices lies the <scene name='90/906893/Binding_pocket/1'>binding pocket</scene>. The binding pocket is comprised of a <scene name='90/906893/Hydrophobic/2'>hydrophobic region</scene> containing <scene name='90/906893/Active_site/7'>two hydrophilic residues</scene>, N80 and Y139, that interact with substrates. The hydrophobic pocket provides specificity to the region while 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.
+Within the four transmembrane helices lies the <scene name='90/906893/Binding_pocket/1'>binding pocket</scene>. The binding pocket is comprised of a <scene name='90/906893/Hydrophobic/2'>hydrophobic region</scene> containing <scene name='90/906893/Active_site/7'>two hydrophilic residues</scene>, N80 and Y139, that interact with substrates. The hydrophobic pocket provides specificity to the region while 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='90/904314/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.
 ==Catalytic Mechanism of VKOR==