English: "Detailed view of the α2 hook (coloured in orange with the residue carbons in yellow) and its interaction with residues at the AMP-3 site on the γ-subunit (coloured pink with the residue carbons in grey) and with a loop from the β-subunit (coloured green with the carbons in grey). AMP-3 is shown in stick representation (with the carbons coloured in grey). His-366(α2-hook) forms a salt bridge with Glu-296(γ), while the following proline at position 367 introduces a kink into the chain, which seems instrumental in positioning Glu-368(α2-hook) that makes salt-bridges to Lys-170(γ) and Arg-70(γ). Arg-369(α2-hook) makes hydrogen bonds with three residues on a loop from the β-subunit, Thr-219(β), and the main-chain carbonyl oxygen of Gly-220(β). Potential interactions are indicated by a thin dashed blue line." Figure 4b from B.Xiao et al. "Structural basis of AMPK regulation by small molecule activators" Nature Communications 4 doi:10.1038/ncomms4017 . Image and description copied under CC-BY 3.0 licence.