The structure of the tautomeric form N1H of carnosine (β-alanine-L- histidine) complex with the active site of soluble guanylate cyclase was investigated based on molecular mechanics, quantum chemistry, and molecular docking methods. It was shown that carnosine binding occurs in a region close to the heme pocket of guanylate cyclase and is characterized by a binding affinity of about -4.5 kcal/mol. The obtained results may be useful for predicting and using carnosine and its analogues as inhibitors of soluble guanylate cyclase for the development of new therapeutic drugs.