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. 2020 Jan 30;11:620. doi: 10.1038/s41467-020-14484-w

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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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — a Electron density detected in two clefts on the surface of the Bateman domain of each monomer in the ASU was assigned to the coordination of one ATP and one GMP molecule in the canonical nucleotide binding sites. b, c Detailed view of the ATP and GMP binding. The protein is shown as green cartoons and the nucleotides as gray sticks. The side chain of Lys157’ from the neighboring monomer is colored in blue. The ATP and GMP as well as interacting residues are displayed as sticks. Yellow dashes represent hydrogen bonds. d Superposition of the second canonical binding site of TbIMPDH-ATP1/GMP2 (green) with that of AgIMPDH-ATP1/ATP2 (gray). Due to the flipped binding mode of GMP2 in TbIMPDH, the side chain of Arg219 occupies the space required for the phosphate groups of ATP2 in AgIMPDH. In b–d, the displayed 2F_oF_c-electron density is countered at 1.0 sigma.