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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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Close up of the binding site with residues of the catalytic centre. Catalytic residues (red) with bound sinigrin (magenta), PAP (cyan) and protein surface (light grey). Several atomic positions occupied by the polar groups of sinigrin in the AtSOT18•PAP•sinigrin complex, including the sulphate moiety, are filled with solvent molecules (water: blue spheres; ethane-1,2-diol: green sticks) in the AtSOT18•PAP complex structure.