To analyze the stability of the lactate-acetyl CoA complex, the MD simulations were carried out for a length of 20 ns. For comparison, a known substrate acetate is selected as a positive control for MD simulations of acetyl-CoA synthetase. We have analyzed the conformation of the protein-ligand complex obtained during the simulation period of 20ns. Root mean square deviation (RMSD) was calculated during the simulation trajectory of 20ns for the ligands such as lactate and acetate against acetyl-CoA synthetase. The RMSD evolution plot of acetyl-CoA synthetase on the Y-axis suggests that values (1.2 to 2.4 Å) for lactate (Figure ) is within the well-accepted range, 1-3 Å and almost similar to acetate (Figure ) RMSD value (0.9 to 2.7 Å) Furthermore, it is important to note that simulations are converged and appear to be stabilized at the end of simulations of length between 12 to 20 ns for lactate and a known substrate of acetyl-CoA synthetase.