To understand the mode of binding of Lamellarin H and assess its affinity, we carried out a hydrogen bond analysis to investigate the capability of the compound to elicit and maintain different hydrogen bonds within the pocket. The cutoff distance for the Indeed, for a more robust binding affinity assessment, we ran free energy calculations for the complex along with a decomposition analysis for the residues within 6 Å from the ligand to indicate the high interacting pocket residues responsible for the possible inhibition activity of the lamellarin H . the following (Table ) shows the calculated different energy terms with the total free energy term calculated for Lamellarin H bound to SARS-CoV-2 Mpro. Those values are also plotted in Figure . Through the energy decomposition analysis, six residues within the pocket were indicated to be highly interacting with lamellarin H . These residues are ASN142, GLU166, ASP187, ARG188, GLN189, and GLN 192. Furthermore, their energy contributions, along with the other residues within 6 Å from the ligand are plotted in