In this direction, we have employed in silico approach to understanding the epigenetic modification by the process of lactylation. Autodock Vina was used to perform molecular docking experiments due to its better accuracy in predicting binding patterns, less run time, higher reproducibility, and its ability to powerfully search for potential energy surfaces . The molecular binding patterns of lactyl-CoA and acetyl-CoA against HAT p300 showed similar attributes in terms of binding energy and interacting amino acid residues (Table ). DSV3 was used after molecular docking to find the binding residues and details of polar bonds including hydrogen bonds. Lactyl-CoA binds through six strong conventional hydrogen bonds to the binding residues ARG1312, GLU1423, LYS1426, LYS1427, GLU1477, ARG1478) of HAT p300 protein (Figure and Figure , Table ). The binding affinity (-9.6 kcal/mol) and specificity of lactyl-CoA within the active site of HAT p300 shared almost identical binding attributes such as docking energy (-10.3 kcal/mol) and key residues (ARG1305, ASP1306, ARG1312, GLU1416, GLU1423, GLU1477, ARG1478) responsible for hydrogen bonds for a stable acetyl-CoA and HAT p300 enzyme complex (Figure and Figure ). Molecular interactions suggested that lactyl-CoA may display equivalent binding affinity that occupies the similar binding pocket of acetyl-CoA in the substrate binding site of the HAT p300 enzyme.