The tuberculosis (TB) affects world population drastically and is responsible for 1.5 million deaths and 8 million new cases per year. The bacterium, Mycobacterium tuberculosis, causing tuberculosis in Homo sapiens can persist in the host and escape from an intact immune response. The pathogenicity of bacteria is due to mycolic acids, long chain fatty acids and lipids containing methyl branched fatty acids. The lipids synthesis involves multifunctional enzymes namely polyketide synthases (PKS) and two fatty acid synthase (FAS) systems. The attachment of 49-phosphopantetheine group from Coenzyme A (CoA) is catalyzed by phosphopantetheinyl transferase (PPTase) enzymes which convert from its inactive apo form to functional holo form. Two PPTases in mycobacteria namely AcpS and PptT are highly conserved and activates specific protein substrate in bacterium. The enzyme PptT is found to be a novel drug target and is mainly involved in the assembly of mycobactin which is required for virulence, by activating two non-ribosomal synthethases (NRPS) namely MbtB and MbtE. PptT plays a critical role in development of Mycobacterium tuberculosis by providing synthesis of components that is needed for the growth and also others factors involved in virulence. The enzyme Phosphopantetheinyl transferase is an attractive drug target as it is primarily involved in post translational modification of various types-I polyketide synthases and assembly of mycobactin, which is required for lipid virulence factors. The aim of the present study is to construct the 3D model for PptT and to find the active site and to design novel inhibitors using in silico studies like homology modeling and Molecular docking towards tuberculosis treatment.