Leishmania major methionyl-tRNA synthetase was another Leishmania protein target with good docking energies. Although the docking energies with this protein were excellent (average Edock = −106.9 kJ/mol), they are much poorer than the docking energy of the normal substrate, methionyl adenylate (Edock = −168.1 kJ/mol). Similarly, the T. cruzi target protein with the best docking was UDP-galactose mutase (average Edock = −104.5 kJ/mol), but the normal substrate and co-crystallized ligand, uridine diphosphate (UDP), had a much superior docking energy (Edock = −232.8 kJ/mol). Likewise, L. major UDP-glucose pyrophosphorylase showed an average docking energy of −99.9 kJ/mol, which was much worse than UDP itself (Edock = −145.9 kJ/mol). The diterpenoids showed good docking to T. cruzi spermidine synthase, with an average docking energy of −96.8 kJ/mol; however, these are much worse than the docking energy of the co-crystallized ligand, S-adenosyl methionine, with a docking energy of −133.0 kJ/mol. Thus, although they exhibited good docking properties, it is unlikely that Copaifera diterpenoids can compete with the normal substrate ligands for these proteins.