Table 1.

The results of molecular docking of the P(-)C(-)-isomer of soman into the possible sites of phosphonylation or esterase activity of albumin.

Binding Site	Kd, μM	Dist (P-O(N)), nm	Amino Acid Closest to the Ligand	Distance to the Closest Amino Acid, nm	Acetylation by p-Nitrophenyl Acetate [25]
Tyr411	601 ± 26	0.72	-	-	+
Tyr150	280 ± 3	0.36	-	-	-
Ser192	581 ± 10	1.06	Ser193	0.38	+
Ser193	518 ± 14	0.38	-	-	-
Thr243	290 ± 6	1.28	Tyr150	0.35	-
Ser287	295 ± 15	0.77	Tyr150	0.36	+
Lys402	737 ± 27	0.37	-	-	+
Ser454	572 ± 17	1.14	Tyr411	0.71	+
Thr540	759 ± 21	0.87	Lys402	0.37	+

K_d—the dissociation constant of an obtained complex;dist (P-O(N))—the distance between the phosphorus atom of soman and the hydroxyl oxygen atom (nitrogen in the case of lysine) of an amino acid studied.