In silico docking of herbal based 'epigallocatechin' onto homology modeled ketoacyl-ACP reductase domain of FAS protein from Mycobacterium tuberculosis H37Rv

In the present study, tertiary structure of ketoacyl-ACP reductase (KR) domain of FAS II protein from Mycobacterium tuberculosis H37Rv has been predicted using MODELLER as well as SWISS MODEL server. Of all the models generated, the one built by MODELLER using 2UV8_A as the template was of superior quality. Based on the structural coordinates of KR model submitted to POCKETFINDER, several ligand binding sites were identified, which were useful for undertaking docking studies. Docking of homology modeled KR domain with 'isoniazid' (synthetic) and 'epigallocatechin' (EGC) from green tea suggests that EGC had a higher binding affinity to the protein than the synthetic drug isoniazid. Thus, the present in silico study provides a very strong basis for exploring herbal based drug molecules as alternative to synthetic drugs to combat multi-drug resistant strains of M. tuberculosis.