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. 2020 Feb 21;10:3195. doi: 10.1038/s41598-020-60263-4

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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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(A) Cartoon structure of Tt1001 protein. α-helix, β-sheet and loops were colored in red, yellow and green, respectively. P-loop was highlighted in marine. (B) Essential residues Cys11, Cys16, Arg17 and Asp123 were showed as sticks. (C) Tryptophan and tyrosine residues were showed as sticks and lines, respectively. (D) Polar and charged residues located on loop 3 and loop 5 are showed as sticks. All the structures are prepared by PyMOL (DeLano, Warren L., The PyMOL Molecular Graphics System (2008). DeLano Scientific, California, USA).