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. Author manuscript; available in PMC: 2019 May 12.
Published in final edited form as: Nat Chem Biol. 2018 Nov 12;14(12):1150–1158. doi: 10.1038/s41589-018-0152-y

Figure 4.

Figure 4

Binding mode of the M2 receptor to AF-DX 384. (a) Superposition of the S110R mutant bound to NMS (gray) and AF-DX 384 (magenta). The extracellular end of TM5 in the AF-DX 384–bound structure is 3.5 Å away from its position in the NMS-bound structure. The side chains of the residues in the AF-DX 384–bound structure are colored in orange. (b) In the AF-DX 384–bound structure, D1033.32 interacts with two nitrogen atoms of AF-DX 384. (c) Both Y1043.33 and Y4036.51 form hydrogen bonds with the oxygen atom of N-ethylamide. (d) The distance between AF-DX 384 and the arginine residue at the position 3.39.