Sandbox Reserved 1805: Difference between revisions

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== Other Important Features ==

MqnA is a homodimer composed of two molecules connected by linkers that lead to beta sheets which then lead to alpha helices. This structure drives function by allowing it to maintain its specific venus flytrap fold conformation when bound to the ligand. Finally, when considering the main product of the reaction, 3-EPB it is important to know that the substrate's binding site is only partially occupied in the less ordered orthorhombic chain A, suggesting that 3-EPB binding draws residues of lobe 2 toward the active site." ~~Orthombic~~ chain A also had less electron density, meaning it could take more than one conformation.

MqnA is a homodimer composed of two molecules connected by linkers that lead to beta sheets which then lead to alpha helices. This structure drives function by allowing it to maintain its specific venus flytrap fold conformation when bound to the ligand. Finally, when considering the main product of the reaction, 3-EPB it is important to know that the substrate's binding site is only partially occupied in the less ordered orthorhombic chain A, suggesting that 3-EPB binding draws residues of lobe 2 toward the active site." Orthorhombic chain A also had less electron density, meaning it could take more than one conformation.

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.

</StructureSection>

== References ==

Sandbox Reserved 1805: Difference between revisions

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 == Other Important Features ==
-MqnA is a homodimer composed of two molecules connected by linkers that lead to beta sheets which then lead to alpha helices. This structure drives function by allowing it to maintain its specific venus flytrap fold conformation when bound to the ligand. Finally, when considering the main product of the reaction, 3-EPB it is important to know that the substrate's binding site is only partially occupied in the less ordered orthorhombic chain A, suggesting that 3-EPB binding draws residues of lobe 2 toward the active site." Orthombic chain A also had less electron density, meaning it could take more than one conformation.
+MqnA is a homodimer composed of two molecules connected by linkers that lead to beta sheets which then lead to alpha helices. This structure drives function by allowing it to maintain its specific venus flytrap fold conformation when bound to the ligand. Finally, when considering the main product of the reaction, 3-EPB it is important to know that the substrate's binding site is only partially occupied in the less ordered orthorhombic chain A, suggesting that 3-EPB binding draws residues of lobe 2 toward the active site." Orthorhombic chain A also had less electron density, meaning it could take more than one conformation.
-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.
 </StructureSection>
 == References ==
 <ref>9672406</ref>