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Literature summary for 1.3.1.9 extracted from
- Conformational changes in 2-trans-enoyl-ACP (CoA) reductase (InhA) from M. tuberculosis induced by an inorganic complex: a molecular dynamics simulation study (2012), J. Mol. Model., 18, 1779-1790.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| I21V | mutant resistant to isoniazid | Mycobacterium tuberculosis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| pentacyano(isoniazid)ferrate(II) | inhibits both wild-type and isoniazid-resistant I21V mutants of InhA. Inactivation does not require activation by KatG. Compound strongly interacts with InhA, the interactions lead to macromolecular instabilities reflected in the long time necessary for simulation convergence. The instabilities are mainly due to perturbation of the substrate binding loop, particularly the partial denaturation of helices alpha6 and alpha7. The association of the inhibitor with enzyme is very strong in the first 20.0 ns, but becomes very week at the end of the moleculár dynamics simulation | Mycobacterium tuberculosis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
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