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. 2021 May 4;11:9453. doi: 10.1038/s41598-021-88672-z

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© The Author(s) 2021

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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Comparison of the AcCoA donor sites of E. anophelis CatB and V. cholerae catB7 proteins. (A) Superimposed structure of E. anophelis CatB (6MFK) and V. cholerae catB9 (6U9C²⁷) trimer. Zoomed view to show residues surrounding AcCoA, shown in yellow sticks. (B) Putative active site residues of E. anophelis and V. cholerae CAT proteins found within the AcCoA binding site. (C) Diagram of hydrogen bonds between putative active site residues of the E. anophelis and V. cholerae CAT proteins and AcCoA molecule. (D) CatB putative active site cavity where AcCoA binds; residues important for H-bonding are coloured in red. AcCoA is in yellow sticks and is modeled from the V. cholerae 6U9C²⁷ structure.