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. 2020 Sep 28;10:15917. doi: 10.1038/s41598-020-72528-z

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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 TMPRSS2 active site is highly conserved among species. (A) Cartoon representation of hTMPRSS2, with the SRCR domain in beige and the Peptidase S1 domain in teal. In the close-up panels the catalytic triad (H296, D345 and S441) is shown in violet sticks and molecular surface colored by electrostatic potential (from − 44 kT/e (red) to 44 kT/e (blue)). A pink dotted line has been placed in the Peptidase S1 active pocket. (B) Multiple sequences alignment of hTMPRSS2, cavTMPRSS2, dogTMPRSS2, catTMPRSS2, ratTMPRSS2, rabTMPRSS2, ferTMPRSS2, musTMPRSS2. Peptidase S1 active pocket residues have been highlighted in red with the relative consensus sequence. Catalytic triad residues are shown in red in the consensus sequence.