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. 2019 Dec 27;9:19825. doi: 10.1038/s41598-019-56081-y

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Structural context of target titratable residues. (a) Single subunit of the cryo-EM structure of the hERG1a channel²⁴ with transmembrane domains labelled. Regions of extracellular loops colored white are absent in the cryoEM structure (PDB:5VA1)²⁴ and were modelled into the structure using Modeller v9.17³⁴ (https://salilab.org/modeller/). The region enclosed in the dashed box comprises most of the extracellular turret between helices S5 and S6, and is expanded in (b). (c) Location of the E575/H578 pair mapped onto the electrostatic surface (at pH 7.4; 0.15 mM NaCl) on the extracellular side of the hERG1a channel. (d) The E575/H578 motif is linked via an E575 (on S5) –T634 (S6) charge/hydrogen bond interaction to a hydrogen-bonded network involving N633, S631 with N629 on adjacent subunits of the hERG1a channel that forms a ring around the top of the selectivity filter (SF).