The total non-bonded interaction energy was found to -197.7 kJ/mol for NSp16-2-DG(6wkq-2-DG), hence the most favourable interaction of ligand 2-DG occurs with O-methyl transferase (NSp-16) of SARS-CoV-2. Total non-bonded interaction energy for 3CL pro -2-DG(6lu7-2-DG), RdRp-2-DG(7bv1-2-DG) and PL pro -2-DG(6wuu-2-DG) are found to be -97.1 kJ/mol, -66.2 kJ/mol and -10.3 kJ/mol respectively (Table ). These energy values predict that only in NSp16(6wkq) the ligand 2-DG is stable and tends to be in the binding site. However, for the other three viral proteins 3CL pro , RdRp and PL pro the interaction energy is much lower to stabilise the ligand in the binding cavity. The next section of MD analysis is the centre of mass distance which calculates the distance between the centre of mass of the residues in the binding site with the centre of mass of the ligand. Average centre of mass distance if larger than 1 nm would predict the ligand has escaped the binding pocket after MD simulation.