Molecular docking is a powerful and significant approach for the identification of lead molecules on the basis of virtual screening. With this a large number of compounds can be tested and based on the scoring function and ranking, the conclusion can be made that how the selected compounds can inhibit the targeted protein/receptor. By keeping in view, the importance of selective inhibitors of cholinesterase in the treatment of Alzheimer disease, here we are focused on the determination of the mechanism of binding interactions of few benzene-1,3-diol derivatives within the active site of both acetyl-cholinesterase (AChE) and butyrylcholinesterase (BChE). All the selective ligands were found to have a greater binding affinity with the BChE as compared to that of AChE, by an average value of ~?28.4 and ~?12.5 kJ/mol, respectively. The results suggested that the identified inhibitors can be used as the lead candidates for the development of novel inhibitors of the targeted enzymes against specific diseases, thus opening the possibility of new therapeutic strategies.