Table 3. Residues of MAP2k and TGFβ Interacting with the Known and Predicted Ligands in Their Best-Docked Poses.

			types of interactions and residues involved (premolecular dynamic simulations)
protein	ligand	molecular docking (kcal/mol)	H-bonds	hydrophobic, polar, and π–π stacking
MAP2k	CID135398122a	–4.483	Asp277	Met142
	CHEMBL287306	–6.691	Asp277	Lys165
	CHEMBL361297	–9.324	Asp277, Met215, Lys165	Gly148, Ser276, Ser263, Leu266, Met142
	CHEMBL1242568	–7.332	Asp277, Met215
TGFβ	DB02010a	–9.345	His283, Asn287, Asp281	Val211, Asn287, Lys337
	CHEMBL1852770	–7.417	His283, Asp351, Cys350	Glu245, Phe352, Lys232, Ala230
	CHEMBL1762790	–10.876	Asp351, Glu245, Thr280	Lys213, Leu260, Leu340
	CHEMBL1241768	–9.751	His283, Asp281, Thr280	Ala230, Phe282, Lue260

^aPreviously reported inhibitors in the literature.^30,31