Sandbox Reserved 1559: Difference between revisions

This protein has a  <scene name='82/823083/6ojttriad/1'>Catalytic Triad</scene> which consists of the amino acids Phe-59, Tyr101, and Lys-134. These amino acids play an important role in catalysis for the protein. Lys-134 proved to be the most important amino acid. The basic spacefill view of the entire protein allows for visualization of the different elements in different colors. The elements shown are carbon (Grey), nitrogen (Blue), and oxygen (Red). The <scene name='82/823083/Spacefill/1'>spacefill view</scene> also allows for visualization of different allosteric binding sites. This protein has a <scene name='82/823083/Nsl_ligand/1'>ligand</scene>, called NSL. The structural fold of LsdA is that of a  <scene name='83/830391/Rainbow_7blade_beta_propeller/2'>seven-bladed β-propeller</scene>. <scene name='82/823083/Hydrophobic/1'>Hydrophobic interactions</scene> are highlighted in grey, and polar regions are purple, while the ligand is yellow. This protein has a catalytic triad for binding that consists of tyrosine (hydrophilic), phenylalanine (hydrophobic), and lysine (has a positive charge).

The tertiary structure creates a<scene name='82/823083/Aminobindingpocket/1'> binding pocket of amino acids</scene> 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. LsdA can only cleave 4-hydroxystilbenes. The photo below shows the NSL ligand interacting in the binding pocket.