In order to provide some insight into the mechanisms of activity, a virtual screening of copaiba diterpenoids has been carried out against several bacterial protein targets, including peptide deformylase, DNA gyrase, topoisomerase IV, UDP-galactopyranose mutase, protein tyrosine phosphatase, cytochrome P450 CYP 121, and nicotinamide adenine dinucleotide (NAD+)-dependent DNA ligase  (see Table 6). The best bacterial target for copalic acid was Mycobacterium tuberculosis DNA gyrase B (PDB 3ZKD) with a docking energy (Edock) of −105.7 kJ/mol. The protein with the best docking energy with kaurenoic acid was S. pneumoniae peptide deformylase (PDB 2AIE, Edock = −89.7 kJ/mol). 3α-Alepterolic acid acetate was the best docking ligand to Escherichia coli topoisomerase IV (PDB 1S16) and M. tuberculosis DNAGyrB (PDB 3ZKD) with docking energies of −118.8 and −118.3 kJ/mol, respectively. 3β-Alepterolic acid acetate also showed excellent docking to these two proteins with docking energies of −117.1 and −117.3 kJ/mol, respectively. The best bacterial target for ent-polyalthic acid was M. tuberculosis protein tyrosine phosphatase (PDB 2OZ5, Edock = −107.2 kJ/mol). The copaiba diterpenoid ligand with the best docking properties was 7α-acetoxyhardwickiic acid with S. aureus peptide deformylase (PDB 3U7M, Edock = −120.6 kJ/mol).