Table 4.

Molecular docking results of all ligands in complex with SRC, and AKT1.

Protein	Ligand	Binding energy (kcal/mol)	Hydrogen bonds	Hydrophobic interactions
SRC	F	− 10.7	Lys298, Ser348	Leu276, Gly277, Gly347, Leu350, Asp351, Gln278, Gly279, Val284, Thr341, Ala296, Arg391, Ala393, Leu396, Asp407
	G	− 9.2	Cys280	Gln278, Leu276, Gly279, Val284, Lys298, Thr341, Gly347, Ser348, Ala393, Leu396, Ala406, Asp407
	Control	− 9.4	Asp389	Leu276, Gly279, Phe281, Gly282, Glu283, Val284, Ala296, Lys298, Tyr343, Met344, Ser348, Gly347, Leu396, Asp407, Ala411, Leu410, Ile414
AKT1	F	− 10.7	N/A	Asn53, Gln79, Trp80, Thr82, Ile84, Ser205, Leu210, Thr211, Val270, Val271, Tyr272, Asp274, Thr291, Asp292, Gly294
	G	− 11.7	Lys268	Asn53, Asn54, Gln79, Trp80, Thr82, Gln203, Asn204, Ser205, Leu264, Val270, Val271, Tyr272, Asp274, Thr291, Asp292, Gly294
	Control	− 9.7	Gln79, Thr82, Val271	Trp80, Val270, Tyr272, Arg273, Asp274, Asp292