Sandbox GGC13: Difference between revisions

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The active site contains three different binding pockets to accommodate the substrate, Nicotinamide, and adenine.   
The active site contains three different binding pockets to accommodate the substrate, Nicotinamide, and adenine.   
The substrate binding pocket relies on heavily on hydrogen binding and ionic interactions in order to effectively bind the substrate.  Upon binding, the substrate binding pocket undergoes a conformational change where interactions between the substrate or inhibitor and a glutamine residue (Q99) essentially pull the active loop closed. <ref>DOI 10.3390/molecules22122217</ref>
The substrate binding pocket relies on heavily on hydrogen binding and ionic interactions in order to effectively bind the substrate.  Upon binding, the substrate binding pocket undergoes a conformational change where interactions between the substrate or inhibitor and a glutamine residue (Q99) essentially pull the active loop closed. <ref>DOI 10.3390/molecules22122217</ref>
<scene name='78/781197/Oxamate/3'>Close up interactions between the substrate binding pocket and the inhibitor, oxamate.  The substrate active site to which oxamate is bound is in the closed conformation.</scene>
<scene name='78/781197/Oxamate/4'>Close up interactions between the substrate binding pocket and the inhibitor, oxamate.  The substrate active site to which oxamate is bound is in the closed conformation.</scene>