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. 2018 Feb 9;8:2714. doi: 10.1038/s41598-018-21056-y

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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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Three-dimensional structure of PmDAP IV. The catalytic domain is coloured in magenta. The β-propeller domain is coloured from purple (blade-1) to red (blade-8). A long insertion containing Arg106 located between blade-1 and blade-2, which was disordered in the ligand-free form, is shown in gold. (A) Dimeric structure of PmDAP IV. (B) PmDAP IV subunit. The catalytic triad “Ser613, Asp689, and His721”, the double-Glu motif “Glu208-Glu209”, Arg106 located between blade-1 and blade-2, a bound inhibitor molecule, and blades 1 to 4 are labelled.