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. 2020 Jun 23;10:10205. doi: 10.1038/s41598-020-66431-w

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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 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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The apo structure of Glu166Tyr reveals an extensive hydrogen bonding network for Tyr166 and a centrally located water molecule in the active site. (a) Tyr166 forms a network of hydrogen bonds with other key catalytic residues and a hydrolytic water molecule (WAT_Nu) in the active site. Fo-Fc omit map (purple) is drawn in mesh format and contoured at 2.0 σ. The dashed lines indicate hydrogen bonds. (b) Superposition of Glu166Tyr active site (cyan) with that of the wild-type (golden). WAT_Nu: the putative hydrolytic water molecule in the wild-type structure. Figures are made using CCP4mg.