Sandbox Reserved 1759: Difference between revisions

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== Important amino acids==

The <scene name='93/934003/Ligand/2'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.

The <scene name='93/934003/Ligand/3'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/3'>Lys94, Tyr99, Arg128, and Glu138</scene>.

== Structural highlights ==

Sandbox Reserved 1759: Difference between revisions

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@@ Line 13: / Line 13: @@
 == Important amino acids==
-The <scene name='93/934003/Ligand/2'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/1'>Lys94, Tyr99, Arg128, and Glu138</scene>.
+The <scene name='93/934003/Ligand/3'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128/3'>Arg128</scene>. In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well. Amino acids residue aspartate is important for catalytic activity and the stability of the protein. When <scene name='93/934003/Asp309/3'>Asp309</scene> is replaced the enzyme experiences complete loss of MBD activity. The internal surface of the ligand binding cavity consists of mostly non-polar amino acids. The cavity opening is mostly polar amino acids, such as <scene name='93/934003/Cavity_polar_residue/3'>Lys94, Tyr99, Arg128, and Glu138</scene>.
 == Structural highlights ==