Studying the three-dimensional structure of peptide molecules is important when creat-ing new drugs. Peptides are the human body’s own resource. Understand the mecha-nism of action of these molecules can be, if you solve the problem of their structural and functional activity. Nociceptins are a new type of regulatory peptides of medical interest. Natural nociceptin reduces motor activity, causes a stress response and modu-lates spatial attention. This work is devoted to determining the spatial structure and conformational possibilities of the heptapeptide molecule with the amino acid sequence H-Phe1-Gly2-Gly3-Phe4-Pro5-Gly6-Pro7-OH. It is one of the recently synthesized ana-logues of nociceptin. It was found that the N-terminal tripeptide and tetrapeptide of this molecule are active and very important. Using the method of molecular mechanics, the spatial structure and conformational properties of the heptapeptide molecule were determined. The potential energy of this molecule was estimated as the sum of non-valent, electrostatic, torsion interactions and the energy of hydrogen bonds. 11 low-energy conformations were found for heptapeptide, the values of the dihedral angles of the main and side chains, and the energy of intra- and inter-residue interactions was estimated. It is revealed that low energy conformations of this molecule have the half-folded and folded type of backbone. The side chains of the Phe1 and Phe4 amino acids in low-energy conformations carry out effective interactions and are conformationally labile amino acids, they bring together the regions of the main chain and the side chains of the amino acids included in the heptapeptide. These folded forms bring parts of the backbone and the side chains of the amino acids together, and they result in convenient interactions.