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. Author manuscript; available in PMC: 2022 Apr 1.

Published in final edited form as: Bioorg Chem. 2021 Feb 9;109:104702. doi: 10.1016/j.bioorg.2021.104702

Fig. 6. — The binding modes of NCP_KOR^active, NCP_MOR^active, compound 6c_KOR^active, and compound 6c_MOR^inactive complexes after 100 ns MD simulations. The receptors were shown as cartoon models, the active KOR in light-pink, the active MOR in light-blue, and the inactive MOR in light-green. NCP, compound 6c, and key amino acid residues were shown as stick models. Carbon atoms: NCP in cyan; compound 6c in yellow; key amino acid residues of the KOR in magenta, and the MOR in orange. The dashed lines in yellow represented potential water-mediated hydrogen bonds. The key residues at the allosteric site of the MOR were shown as stick and ball models in magentas. The key residues at the allosteric site of the KOR were shown as stick and ball models in orange. The water molecules were shown as sphere models in red.

Fig. 6. — The binding modes of NCP_KOR^active, NCP_MOR^active, compound 6c_KOR^active, and compound 6c_MOR^inactive complexes after 100 ns MD simulations. The receptors were shown as cartoon models, the active KOR in light-pink, the active MOR in light-blue, and the inactive MOR in light-green. NCP, compound 6c, and key amino acid residues were shown as stick models. Carbon atoms: NCP in cyan; compound 6c in yellow; key amino acid residues of the KOR in magenta, and the MOR in orange. The dashed lines in yellow represented potential water-mediated hydrogen bonds. The key residues at the allosteric site of the MOR were shown as stick and ball models in magentas. The key residues at the allosteric site of the KOR were shown as stick and ball models in orange. The water molecules were shown as sphere models in red.