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98 PROCEEDINGS OF INTERNATIONAL SCIENTIFIC CONFERENCE ON APPLIED BIOTECHNOLOGYFigure 2. The 2D and 3D interactions of %u03b1-pinene, %u03b2-pinene, myrtenyl acetate, and streptomycin in the active sites of the 3WCU protein.It is supposed that the antimicrobial action of the studied oil is dependent on the role of the main compounds %u03b1-pinene, myrtenyl acetate, and %u03b2-pinene. Hence, we then considered a molecular docking calculation to view the interactions between these molecules and protein targets. Before evaluating the antimicrobial effect of these major components, re-docking of the co-crystallizer structures was performed, which also serves as a means to validate the docking method. The results showed a significant overlay between the co-crystallizer ligands and the re-docked ligands, ATP and MgADP with root-mean-square distance (RMSD) of 0.865266 %u00c5 and 1.25953 %u00c5 (RMSD < 2%u00c5), respectively [20], demonstrating the reliability of the docking method. Subsequently, three compounds, %u03b1-pinene, %u03b2-pinene, and myrtenyl acetate, along with streptomycin, were required to bind to the binding site (active site) of the S. aureus FtsA and E. faecalis carbamate kinase. The obtained binding affinity data were presented in Table 3, and the complex docking interactions (2D and 3D-illustrations) were illustrated in Figures 2 and 3. As shown in Table 3, the binding affinity values (%u0394G) of the investigated compounds with proteins S. aureus FtsA and E. faecalis carbamate kinase ranged from %u20134.063 to %u20134.953 and %u20135.722 to %u20136.769 kcal/mol, respectively. Among them, the oxygenated monoterpene compound, myrtenyl acetate, exhibited potent inhibitory potential against both proteins, displaying the lowest binding affinity (%u0394G = %u20136.769 kcal/mol for the 3WQU protein) and (%u0394G = %u20134.953 kcal/mol for the 2WE5 protein). The evaluation of ligand-