Protein Variants | Comment | Organism |
---|---|---|
D270N | upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity | Mycobacterium tuberculosis |
D270N/H96A | the protein can still convert its conformation from open state to closed state. The key interactions between NADH and Asn270 disappear with mutation, with loss of protein activity | Mycobacterium tuberculosis |
H96A | upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WQB1 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WQB1 | - |
- |