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. Author manuscript; available in PMC: 2018 Jan 3.
Published in final edited form as: Structure. 2016 Dec 1;25(1):180–187. doi: 10.1016/j.str.2016.11.007

Figure 2. Crystal structures of ELIC showing 2-bromoethanol (BrEtOH) binding sites.

Figure 2

Top views of BrEtOH binding to ELIC in (a) the resting and (b) desensitized states. (c) Side view of BrEtOH binding to ELIC in the desensitized state. The FO-FC omitted electron density maps (green) are contoured at 3.0 σ. The anomalous difference electron maps (magenta) are contoured at (a) 4.0 σ and (b) 5.0 σ for the resting and desensitized ELIC, respectively. (d)–(f) 2FO-FC electron density maps (light blue, contoured at 1.0 σ) of ELIC in a desensitized state showing: (d) two BrEtOH molecules bound to a pocket in the ECD lined by loop A and loop E; (e) the third BrEtOH in the ECD bound to a pocket between loop G and loop F; and (f) a bottom view of BrEtOH bound to the pore near T237(6′). Residues within 4 Å of BrEtOH molecules are shown as sticks. The maps from (a) to (f) all have a carve distance of 2.0 Å from BrEtOH molecules.