Metal complexes of the biologically active Ile-Trp dipeptide are formed by coordinating the Ile-Trp dipeptide with metal ions, most notably iron. These complexes demonstrate potential for medical use because of their immunostimulating and immunomodulating effects, as well as their ability to treat iron and immune deficiencies. We performed DFT/B3LYP calculations, using the 6-31+G(d,p) basis set, on the complex of the dimeric dipeptide Ile-Trp with iron (Fe(II). In this compound, two dipeptides, each consisting of isoleucine (Ile) and tryptophan (Trp), are bound together and chelated by iron. Within the framework of the study, the energies of frontier molecular orbitals, energy gap, chemical reactivity descriptors, atomic charge distribution, and dipole moment were calculated for the Fe-Ile-Trp dimer compound. The data obtained allowed for the accu-rate characterization of the stable molecular structure of the studied system. The calcu-lations revealed that the nature of the mentioned substituent facilitates the formation of two stable, concave ring-shaped cavities through coordination bonds C16–Fe89, N34–Fe89, C60–Fe89, and N78–Fe89 between iron and side chain atoms of Ile and Trp residues. In addition, the effect of hydrogen bonds on the geometric structure of the complex was also observed. So, N21H22... O44 and N65H66 … O88 hydrogen bonds between the hydrogen atom of the amide group and the oxygen atom of the carboxyl group in the monomers formed the pseudo five-membered rings. To identify the loca-tions of electrophilic and nucleophilic sites, or potential molecular interaction zones, the molecular electrostatic potential (MEP) maps of this complex were analyzed. The results allowed for an identification of the potential reactive sites of this compound and as-sessment of the Fe substituent's reactivity and the resulting chemical properties, includ-ing its catalytic and biochemical activity.