Sandbox Reserved 1677: Difference between revisions
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<scene name='87/873239/Rossmann_fold_motifs/2'>The Rossmann fold</scene> of the NAD(H) binding domain provides extensive polar and apolar interactions that position the nicotinamide ring of NAD+ in proximity to the C291A point mutation.Its main function is to bind NAD+ cofactor and contribute to substrate binding. The cleft found in the protein is where the active site is, the binding cleft contains the octanal binding amino acids. This fold is also called a beta alpha beta fold because the beta strands participate in the formation of a beta sheet. | <scene name='87/873239/Rossmann_fold_motifs/2'>The Rossmann fold</scene> of the NAD(H) binding domain provides extensive polar and apolar interactions that position the nicotinamide ring of NAD+ in proximity to the C291A point mutation.Its main function is to bind NAD+ cofactor and contribute to substrate binding. The cleft found in the protein is where the active site is, the binding cleft contains the octanal binding amino acids. This fold is also called a beta alpha beta fold because the beta strands participate in the formation of a beta sheet. | ||
<scene name='87/873239/Interactions/4'>Effects of interactions</scene> | |||
Glu 391 Mutation, loss of Glu 257 side chain removed the internal interaction that helps position the amine group of the nicotinamide and changes at this residue could change the orientation of the nicotinamide group for hydride transfer. | Glu 391 Mutation, loss of Glu 257 side chain removed the internal interaction that helps position the amine group of the nicotinamide and changes at this residue could change the orientation of the nicotinamide group for hydride transfer. | ||
Cysteine is the most important catalytic residues | Cysteine is the most important catalytic residues | ||
