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. 2023 Aug 3;14:4666. doi: 10.1038/s41467-023-40416-5

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© The Author(s) 2023

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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Fig. 4 — a Simplified representation of the 70S ribosome with the AMK binding site indicated with the green star. b The unbiased (F_o – F_c) difference electron density map of AMK bound at the inter-subunit space is contoured at 2.3σ. c AMK interacts with elements of inter-subunit bridge B5, helix h44 of 16S rRNA, helix H64 of 23S rRNA, and ribosomal protein uL14. The amine group of the AHB group forms water-mediated (cyan) H-bonds with the phosphate backbone of h44.