Objectives: The objectives of the research are to use molecular modeling methods to examine the inhibition of the catalase enzyme, to examine the most energetically favorable position of the inhibitor in the enzyme, and to examine the binding of different ligands to catalase. Study Design: The research was done as an in silico study - finding scientific achievements and reducing the set of clinical and laboratory research. Materials and methods: Data on the catalase enzyme were taken from the PDB database, and inhibitor structures were taken from the PubChem database, except for one inhibitor that was created in the Avogadro program. The software program LeDock is used to predict the most energetically favorable position. Structures were visualized using VMD software. Results: Inhibitor III has the lowest binding energy. The amino acid residues that are the same in the binding sites of all four inhibitors are His54, Val53, Tyr337, and Asn127. Conclusion: aminoalkane derivatives are very weak inhibitors of catalase, the most favorable position of inhibitor I is in Try337, Arg51, and Arg91, inhibitor II is in position His54 and Val53, inhibitor III is in position Arg344 and Asn127, and the most favorable position of inhibitor IV is in position Asn127.