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. 2018 Oct 18;8:15458. doi: 10.1038/s41598-018-33453-4

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© The Author(s) 2018

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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(A) Schematic of purine biosynthesis and the potential roles for ZMP as a signaling molecule, notably AMPK activation and SAICAR reported activation of PKM2. (B) The structure of LSN3213128. (C) Panel C illustrates a ribbon diagram of the homodimeric bifunctional protein encoded by the homodimeric ATIC with one monomer in cyan and the other in teal is shown in complex with 5-aminoimidazole-4-carboxyamide ribonucleotide (ZMP) in magenta and LSN3213128 in yellow. Only one formyl transferase active site of the homodimeric bifunctional protein is illustrated. Amino acids which hydrogen bond to LSN3213128 are shown in white. I452, D546 and N547 interact with the isoquinolone. K266, N431 & R451 interact with the sulfonamide. D339 interacts with the hydroxypyrrolidine. Both F541 and G316 make significant van der Waals contacts but are not shown for sake of clarity.