Sandbox Reserved 1568: Difference between revisions
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When you look at the <scene name='82/823092/Spacefill_lsda/1'>spacefill view</scene> of the protein dimer you see that the binding pocket accessibility is very restrictive. | When you look at the <scene name='82/823092/Spacefill_lsda/1'>spacefill view</scene> of the protein dimer you see that the binding pocket accessibility is very restrictive. | ||
<scene name='82/823092/Hydrophobic_spacefill/1'>Hydrophobicity-focused</scene> view of the protein. | This is a <scene name='82/823092/Hydrophobic_spacefill/1'>Hydrophobicity-focused</scene> view of the protein. Overall, there doesn't seem to be any dominant hydrophobic or hydrophillic regions 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 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 <ref>PMID 31292192</ref>. | 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 <ref>PMID 31292192</ref>. | ||
