Analysis of interactions of clinical mutants of catalase-peroxidase (KatG) responsible for isoniazid resistance in Mycobacterium tuberculosis with derivatives of isoniazid

C50 can be considered as a better lead for INH-resistant strains. These models demonstrate the binding interaction of all naturally occurring KatG mutants of MTB at position 315 with derivatives of INH. This information will be helpful for lead compound-based identification of derivatives that may be used against INH-resistant MTB strains and may provide a useful structural framework for designing new antitubercular agents that can circumvent INH resistance.