NDM-1 metallo-�?²-lactamase (class B) is a plasmid-borne zinc metalloenzyme that efficiently hydrolyzes �?²-lactam antibiotics, including carbapenems, rendering them ineffective. Resistance to �?² -lactam antibiotics mediated by metallo-�?²-lactamases is an increasingly worrying clinical problem. Because NDM-1 has been found in several clinically important carbapenem-resistant pathogens, there is a need for inhibitors of this enzyme that could protect broad spectrum antibiotics from hydrolysis and thus extend their utility. In the presented research, the 3D structure of NDM-1 protein was modeled using homology modeling by Modeller9v5. Evaluation of the constructed NDM-1 protein model was done by PROCHECK, WHATCHECK, ERRAT, VERIYFY3D and through ProSA calculations. A compound library screening approach was used to identify compounds from the ZINC Database and characterize NDM-1 inhibitors from a library of active compounds. The strategy employed was divided into two categories, viz. screening and docking. A series of compounds from ZINC Database have been identified as potent inhibitors of NDM-1 metallo-�?²-lactamase.