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. 2018 Sep 28;8:14502. doi: 10.1038/s41598-018-32947-5

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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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Structural characteristics of the protease-inhibitor docking output for PE-BBI and KLKs. The secondary structure of PE-BBI was labelled (N-terminal is blue and C-terminal is red), and the active site (Lys⁹) was shown in stick representation. The disulphide bond was showed in stick representation (Orange). The active site of KLKs were labelled with arrows and highlight (Yellow). (A) Possible interactions model between PE-BBI and KLK4. (B) Possible interactions model between PE-BBI and KLK6. (C) Possible interactions model between PE-BBI and KLK8. (D) Possible interactions model between PE-BBI and KLK10.