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. 2020 Sep 21;10:15402. doi: 10.1038/s41598-020-72373-0

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© The Author(s) 2020

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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The active site of TSP2. (a) Surface vacuum electrostatics of the TSP2 trimer, indicating the location of the active site (rectangular black box). Negatively polar regions are colored red and positively polar region are colored blue. The overall polarity of the active site is negative. (b) The partially transparent molecular surface at the active site, highlighting key active site residues. As can be seen, the interface between the green and cyan molecules forms a cleft. The trimer contains three such clefts at the three subunit interfaces. (c) Stereoscopic representation of active site residues. The distances between the three carboxyl groups of Asp506, Asp571, and Glu578, the candidate catalytic resides that were probed by site-directed mutagenesis, are shown in magenta dash lines. Key salt bridges and hydrogen bond interactions are shown in yellow dash lines. Aromatic groups may interact with the substrate pyranose rings. The chloride bound underneath the active site is shown as green sphere. The trimer subunits are colored differently. The figure was generated using the computer program PyMol v1.8.0.2 (Schrödinger, LLC, https://www.pymol.org).