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. 2018 Sep 5;50(9):116. doi: 10.1038/s12276-018-0141-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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Fig. 6 — a 3D model of Cps2D exhibiting typical BY-kinase-like structure. The red loop highlights the Walker A (WA) motif containing ATP-binding conserved residues and the p-loop (α2–β1). The cyan color indicates the catalytic DxD motif, and the yellow color marks the Walker B (WB) motif. These motifs are essential for the enzymatic activity of tyrosine kinases. b The ADP-bound active site of Cps2D with the conserved L49 and DxD catalytic domain. c Our Cps2D model superimposed over previously reported crystal structures of tyrosine kinase from E. coli (Wzc) and S. aureus (CapB)