Sandbox Reserved 1568: Difference between revisions
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<scene name='82/823092/Hydrophobic_spacefill/1'>Hydrophobicity-focused</scene> view of the protein. | <scene name='82/823092/Hydrophobic_spacefill/1'>Hydrophobicity-focused</scene> view of the protein. | ||
The <scene name='82/823092/Catalytic_triad/2'>catalytic triad</scene> of the binding site consists of Phe59, Tyr101, and Lys134 that | The <scene name='82/823092/Catalytic_triad/2'>catalytic triad</scene> of the binding site consists of Phe59, Tyr101, and Lys134 that interact with the 4-hydroxyphenyl portion of the substrate. The triad importance was tested with specific mutations. A F59H mutation led to 3% efficiency comparable to wildtype LsdA. A Y101F mutation led to 20% efficiency comparable to wildtype LsdA. And a K134M mutation showed no discernible lignostilbene cleavage activity. | ||
Important <scene name='82/823092/Active_site_interactions/1'>interactions in the active site</scene> are shown. Green indicates hydrophobic interactions, blue indicates hydrogen bonding interactions, and the orange nucleotides are specific histidines that support and interact with the metal ion (Fe) in the pocket. These two histidines also contribute to hydrogen bonds in the area. | Important <scene name='82/823092/Active_site_interactions/1'>interactions in the active site</scene> are shown. Green indicates hydrophobic interactions, blue indicates hydrogen bonding interactions, and the orange nucleotides are specific histidines that support and interact with the metal ion (Fe) in the pocket. These two histidines also contribute to hydrogen bonds in the area. | ||
