It is known that albumin is able to cut ester bonds in organophosphates (OPs). Amino acids responsible for esterase and pseudo-esterase activity of albumin towards OPs are still not determined. The purpose of this study is to identify the potential sites of esterase activity of albumin by the example of its interaction with soman using molecular modeling methods. The structures of the protein complexes with soman was determined by molecular docking procedure, the stability of the complexes were simulated using molecular dynamics method. It has been determined that productive sorption of soman near Tyr411 is possible only after deprotonation of the tyrosine. Tyr150 binds soman more efficiently than Tyr411; deprotonation of Tyr150 does not affect the binding efficiency, but affects on the stability of the complexes. The true esterase activity of albumin Tyr150 in relation to soman is proposed. It is shown that Ser193 can also be responsible for the esterase activity of albumin. We hypothesize that deprotonation of catalytic amino acid in one of the sites could be initiated by ligand binding in other sites (allosteric regulation).