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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 Cm acceptor sites from E. anophelis CatB and P. aeruginosa catB7. (A) Superimposed structure of E. anophelis CatB (PDB ID: 6MFK) and P. aeruginosa catB7 (PDB ID: 2XAT²⁹) trimer. Zoomed view to show H-bonding interactions between putative active site residues and Cm. (B) Cm binding site residues of E. anophelis and P. aeruginosa CAT proteins. Cm is shown in gray sticks. (C) Diagram of hydrogen bonds between residues of the E. anophelis and P. aeruginosa CAT proteins and Cm molecule. (D) E. anopheles CatB putative Cm acceptor site cavity. Cm is in gray sticks and residues important for H-bonding are coloured in green. Cm was modeled from the P. aeruginosa 2XAT²⁹ structure.