Surface shallow grooves were proposed as F13L-Tecovirimat docking cavities using different computational docking efforts . However, recent docking studies predicted internal MPXV amino acid residues for Tecovirimat contacts as its most probable binding site, validating their hypothetical interactions by molecular dynamic-docking studies (Table , yellow left). Although the detailed mechanisms of inhibition are unknown, Tecovirimat has been proposed to conformationally disturb the F13L near-canonical phospholipase motif to interfere with its activity . Alternatively, Tecovirimat may still fit other F13L binding cavities to block yet-unknown functions, include other allosteric influences on phospholipase activity or bind to possible F13L complexes with other proteins (i.e, poxviral B5R/B6R) to affect their subcellular location.