Sandbox GGC13: Difference between revisions
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<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/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> | ||
The nicotinamide and adenine binding pockets work together to sufficiently bind NADH. Both binding pockets implement hydrogen bonding and hydrophobic interactions with their ligand fragment. In addition to the interactions within the binding pockets, NADH is also supported by ionic forces between arginine (R99) and the pyrophosphate groups. | |||
<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> | ||
The hydroxyl groups of NADH's ribose fragments interacts with the H-bond network created by the substrate and asparagine (N137). | The hydroxyl groups of NADH's ribose fragments interacts with the H-bond network created by the substrate and asparagine (N137). | ||
