TABLE 3.

Molecular docking studies of compounds emodin and AhR inhibitor CH223191 with AhR.

Comp	Glide energy (kcal/mol)	Amino acid residues (within a radius of 4Ǻ from bound ligand)	H-bond formatting residue and bonds
Emodin	−4.064	Tyr316, Leu310, Tyr278, Glu279, Phe280, Tyr281, Hie282, Ala283, Leu284, Ser286, Glu287, Thr290	Thr290 = 2.160, Glu287 = 1.840
AhR inhibitor	−2.740	Asp251, Ser276, Tyr278, Glu279, Tyr291, Hie292, Ala293, Leu294, Asp295, Ser296, Glu297, Asn298, Thr290, Lys291, His293, Gln294	Thr290 = 2.460