Table 3.

The interaction of docking the isolated compounds (1–4) with key amino acid residues in the binding sites of 4 MAPKs (P38 α, ERK2, JNK& MK3), in comparison to the co-crystallized ligand.

Compound	P38 α MAPK			ERK1/2			JNK1			MK3
	FlexX Score	Amino Acids Interactions	Hyde Assessment/Predicted Ki	FlexX Score	Amino Acids Interactions	Hyde Assessment/Predicted Ki	FlexX Score	Amino Acids Interactions	Hyde Assessment/Predicted Ki	FlexX Score	Amino Acids Interactions	Hyde Assessment/Predicted Ki
Curcumin	−24.639	Gly110, Gly033 Met109, Thr106, Asp 168, Asn155, His107	−34/µM	−21.8	MET 108, Gln105, Glu33, Thr 110, Lys114	−28 /µM	−17.72	Asn 114, Met111, Lys 55, Ile32	−23 /µM	−24.63	Lys73, Met121, Glu119, Glu125	−36/ nM
Physcion	−27.99	Gly110, Met109, Thr106, Ala 111, His107	−33/µM	−22.6	Met 108, Gln 105, Lys 54	−23/ µM	−24.07	Glu 109, Met111, Ile32	−32 /µM	−27.99	Met121, Glu119, Thr186	−24/ µM
Chrysophanol	−27.65	Gly110, Met109, Thr106, Ala 111, His107	−32/µM	−22.5	Gln 105, Asp 106, Met 108, Lys54, Asp167, Tyr36, Gly34, Ile56	−17/ mM	−24.44	Glu 109, Met111, Ile32, Ala53	−30 /µM	−27.65	Met121, Glu119, leu50, leu173	−35 /µM
Hesperidin	−20.03	Gly110, Met109, Thr106, Asp 168, Ser 154	−38/nM	−21.9	Asp 106, Met108, Lys114, Asp111, Tyr36, Glu33, Asn15, Gln105, Ile31	−14/ mM	−13.12	Glu 109, Met111, Ile32, Ser34, Lys55	−24/ µM	−20.03	Glu125, Cys120, Met121, Asp187, Glu 170, Lys 73	−22/ µM
(Co-crystallized ligand)	−30.7	Gly110, Met109 Thr106, Ala 157	−41/nM	−39	Lys 54, Asp 167, Met 108, Thr 110, Tyr-36, Gly34, Ile56	−45/ nM	−29	Ile 32, Met111, Glu 109, Val158, Leu168, Ala53, Val40	−39/ nM	−43.17	Met121, Cys120, Glu 170, Glu 125, leu52	−18 /mM