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. 2017 Jun 23;7:4160. doi: 10.1038/s41598-017-04539-2

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© The Author(s) 2017

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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Overall view of AtSOT18 from two perspectives bound with sinigrin (magenta sticks) and PAP (cyan sticks). Indicated are the four conserved regions (region I: blue; region II: yellow; region III: magenta: region IV: cyan), the three flexible loop regions (black), the catalytic residues (red) and proline 136 (orange). The upper view shows the three flexible loops gating the sinigrin binding site. The view below shows how two of the four typical β-strands are formed by the conserved regions II and III.