Introduction: The misuse of β-lactam antibiotics has led to the development of β-lactamase-producing organisms, which inhibit β-lactam activity by hydrolyzing the peptide bond. This study aims to investigate the inhibitory effect of quercetin, a natural composite and isoquinoline alkaloid, on β-lactamase enzyme action, potentially increasing antibiotic effectiveness. Materials and Methods: This study utilized computational techniques like molecular docking and MD simulation to predict the binding mode and possible conformation poses of quercetin with the OXA-10 β-lactamase enzyme. Autodock software was used for docking, while Gromacs 2019.6 package was used for MD simulations to study molecular complex behavior over time. Results: The outcomes of the molecular docking analysis revealed a favorable interaction between quercetin and the OXA-10 β-lactamase enzyme, as evidenced by a binding energy of -5.95 kcal/mol and a suitable binding mode. MD simulations confirmed the docking results, showing stable hydrogen bonds between Quercetin and OXA-10, as well as comparable RMSD, RMSF, SASA values, and other parameters. Discussion: This research shows the potential of quercetin, a natural compound with multiple medicinal effects, as a possible inhibitor of the class D type β-lactamase OXA-10. Therefore, this study maintains valuable intuition for designing new inhibitors of antimicrobial resistance to combat β-lactamase activity.