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. 2021 Jan 14;11:1274. doi: 10.1038/s41598-020-79649-5

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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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Acetyl-CoA binding site depicted within the tertiary structure the GNAT acetyltransferase from Elizabethkingia anophelis. Top left, shown in cartoon format, α-helices, β-strands, and loops are shown in cyan, red, and magenta, respectively. Acetyl-CoA is depicted in stick mode in black, with associated electron density map (2Fo-Fc) contoured at 1.0σ. The side chains of active site residues Tyr114 and Ser107 are depicted in stick mode. Bottom left, the same structure as above, but shown in surface view and coloured grey to depict the binding cleft. The location of Tyr114 and Ser107 are coloured cyan and magenta respectively. Right panel, schematic of hydrogen bond interactions between GNAT acetyltransferase residues and acetyl-CoA.