Objectives: Use molecular modeling methods to examine acetylcholinesterase inhibition, to examine the most energetically favorable positions of inhibitors in the enzyme and by using the molecular dynamics methods find amino acid residues involved in the binding of inhibitors. Study design: The research was done as an in silico study - building a computer model of enzymes and inhibitors. Materials and methods: AChE enzyme data were taken from the PDB base and β- caryophyllene data were taken from the PubChem base. Two free web servers were used to predict the most energy-efficient position: PatchDock and Haddock. The AmberTools software package was used for protein parameterization and dissolution in water. The AMBER software package was used for system optimization and MD simulation. All structures were visualized using VMD software. Results: The results obtained using the PatchDock server show how β-caryophyllene binds to the AChE dimer and did not suggest binding of inhibitors to amino acid residues that have been experimentally determined to play an important role in ligand binding. Using a Haddock server, the results of β-caryophyllene binding to the A protein chain of the AChE enzyme were obtained, and the results are consistent with experimental data. MD simulations showed that the amino acid residues of the enzyme coordinating enzymes correspond to those in the initial structure (solution No. 1, Haddock). Conclusion: The most energy - efficient position obtained by molecular docking methods matches with positions experimentally determined at the Gly122 and Tyr337 binding sites. Using the molecular dynamics method, the inhibitor is coordinated with amino acid residues corresponding to those in the initial structure: Tyr124, Tyr337 and Gly121.