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 substrate binding, the substrate binding pocket undergoes a conformation change where interactions between the substrate or inhibitor and a glutamine residue (Q99) essentially pull the active loop closed. | The substrate binding pocket relies on heavily on hydrogen binding and ionic interactions in order to effectively bind the substrate. Upon substrate binding, the substrate binding pocket undergoes a conformation change where interactions between the substrate or inhibitor and a glutamine residue (Q99) essentially pull the active loop closed. | ||
<scene name='78/781197/Oxamate/ | <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/Nadh/1'>Close up interactions between the NADH and adenine binding pockets and the cofactor, NADH.</scene> | <scene name='78/781197/Nadh/1'>Close up interactions between the NADH and adenine binding pockets and the cofactor, NADH.</scene> | ||
