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. 2017 Jun 22;7:4066. doi: 10.1038/s41598-017-04403-3

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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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Three-Dimensional modeling of CpsK polymorphic variants. (a) The serotype 2 CpsK protein structure is depicted in yellow ribbon, and the position of amino acid residue 161 was colored in green and labeled. The docked substrate UDP-Gal is shown in sticks with the Gal moiety in pink. (b) Detailed view of the catalytic center of protein CpsK from serotype 1/2 with a cysteine residue at position 161 (C161) in complex with UDP-GalNAc as a substrate. Residues predicted to play a role in substrate binding and stabilization are depicted as capped sticks and labeled. Potential hydrogen bond between C161 and N-acetyl group of GalNAc is represented with a dashed grey line. (c) Same view as in panel a for the catalytic center of protein CpsK from serotype 2 with a tryptophan residue at position 161 (W161) in complex with UDP-Gal molecule as a substrate. Dashed grey line represents the potential hydrogen bond between W161 and the hydroxyl group of Gal.