This article explores the possible role of Montelukast in management of SARS-CoV-2 infection after reviewing the available literature and further uses computational docking to estimate the effects of Montelukast on the main protease inhibitor site of SARS-CoV-2.Methodology: In this study, we used molecular docking to estimate the direct effects of Montelukast on the main protease (Mpro) inhibitor site of the SARS-CoV-2. While other studies have been performed on the homology models, we obtained the Mpro crystalized structure, A-chain (304 amino acid residues) from protein data bank (PDB code 5REK) for this analysisResults:The best docked Montelukast conformer had a mfscore of -71.68 and was seen to be making multiple hydrogen bonds with the neighbouring residues (T24, T24, T26, S46) with the closest bond with T24 (Distance= 1.71 angstrom). Important finding was its hydrogen bond with H41 and hydrophobic interactions with C145 as these residues for important members of the active catalytics site.Conclusion:The computational model which was used against the crystalized Mpro structure suggested a possible inhibitory role of Montelukast in binding to the Mpro catalytic site which may modulate and inhibit the viral replication.