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Mycobacterium tuberculosis (Mtb) is the pathogen, which causes tuberculosis. The development of multidrug-resistant and extensively drug-resistant strains in Mtb is due to an efflux mechanism of antibiotics in the bacteria. The efflux pump proteins in the bacteria are implicated in the active efflux of antibiotics. The efflux pump protein, "fluoroquinolones export ATP-binding protein Rv2688c" (FEAB), is considered as a potential therapeutic target to prevent tuberculosis. In the present work, in silico protocols are applied to identify inhibitors for the FEAB protein to arrest the efflux mechanism. Comparative modeling techniques are used to build the protein structure. The generated structure consists of 9 helices, 13 beta strands, and 3 β sheets. The active site is predicted using active site prediction server tools. The virtual screening protocols are carried out to generate small ligand inhibitor structures. The identified ligand molecules show selective binding with Ser97, Glu99, Lys149, Asp171, Glu172, and Ser175 amino acid residues of the protein. The ligand molecules are subjected to in silico prediction of pharmaco kinetic properties, and the predicted IC (HERG) of all the molecules are less than -5.0, which is indicative of the identified ligand molecules is being potentially good FEAB inhibitors.