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. 2016 Nov 7;113(47):E7399–E7408. doi: 10.1073/pnas.1614688113

Fig. 7.

Fig. 7.

Cl binding sites observed in BEST1 are absent in prokaryotic KpBest. Structures are depicted similarly to Fig. 5A with two subunits shown. Cl binding sites (magenta spheres, the three sites for each subunit are shown) in BEST1 (Left) are located at the N-terminal ends of α-helices. KpBest (Right) has continuous α-helices in the corresponding locations (arrows) and does not contain these sites. Ca2+ ions in BEST1 are depicted as teal spheres.