Sandbox Reserved 1559: Difference between revisions
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The flat surface of the B-sheet is pushing the amino acids up, making it possible for the <scene name='82/823083/6ojttriad/1'>catalytic triad</scene> Phe59, Tyr101, and Lys134 to create interactions with the <scene name='82/823083/Nsl_ligand/1'>ligand</scene>. | The flat surface of the B-sheet is pushing the amino acids up, making it possible for the <scene name='82/823083/6ojttriad/1'>catalytic triad</scene> Phe59, Tyr101, and Lys134 to create interactions with the <scene name='82/823083/Nsl_ligand/1'>ligand</scene>. | ||
The tertiary structure creates a binding pocket of amino acids that are important to the active site. His282 provides pi-stacking, Phe305 provides Hydrophobic contacts, and Tyr101 provides Hydrogen bonding. The tertiary structure also allows the NSL ligand to interact using its 4-hydroxy with the catalytic triad. | |||
[[Image:6ojtsecondarystructure.png|600 px]] | [[Image:6ojtsecondarystructure.png|600 px]] | ||
