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. 2021 Sep 6;12:5254. doi: 10.1038/s41467-021-25574-8

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© The Author(s) 2021

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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Fig. 2 — The panels show the superposition of Pdr5 and four related ABC transporters: a human sterol transporter ABCG5/8 (PDB-ID: 5DO7), b human multi-drug transporter ABCG2 (PDB-ID: 6XVI), c bacterial O-antigen polysaccharide transporter Wzm-Wzt (PDB-ID: 7K2T), d bacterial teichoic acid transporter TarGH (PDB-ID: 6JBH). The r.m.s.d. (root-mean-square deviations) of atomic positions in the amino-acid backbone are, for ABCG5/8: 4.3 Å, ABCG2: 3.9 Å, Wzm-Wzt: 9.2 Å, TarGHL: 14 Å. See also: Supplementary Table 2.