The putative structural model of the Slc26a6 TMDs is similar to the resolved CLC-ec1 TMDs. The putative structure of slc26a6 TMDs was predicted using the 3D-Jury software. (A) The PyMol software was used to generate the model of Slc26a6 TMDs (red/purple) and an overlap with CLC-ec1 crystal structure (yellow). The image on the left shows the dimer configuration, the middle is a magnified image of the TMDs, and the right image is a 90° rotation about the vertical axis. This analysis depicts the high similarity between the TMDs of the two proteins. (B) The predicted position of the Slc26a6 TMD helices. (C) A region within the Slc26a6 TMDs, with a spatial architecture similar to the CLC-ec1 ion-gating domain. The Slc26a6 Y163 and E357 (red) had a putative orientation similar to the CLC-ec1 E148 and Y445 (yellow) that were shown to coordinate Cl⁻ binding (Dutzler et al., 2002). Note that the two sites do not fully overlap because they are located in opposite sides of the inverted repeat structures.