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. 2018 Feb 1;8:2170. doi: 10.1038/s41598-018-19902-0

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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 models of the PcCDA catalytic domain. (A) Model 1, using ClCDA (PDB 2IW0) and AnCDA (PDB 2Y8U) as templates. (B) Model 2, using ClCDA (PDB 2IW0) and VcCDA (PDB 4OUI) as templates. The loops are coloured as in Fig. 4 according to²⁸. (C) Simulated docking of A4 ligand to Model 1, lowest energy binding mode which places the penultimate GlcNAc residue properly oriented for catalysis in subsite 0. (D) Magnification of the active site in Model 1, showing residues Asp¹¹⁵-His¹⁷³-His¹⁷⁷ (metal binding triad), Asp¹¹⁴ (general base), His²⁷⁷ (general acid), and the Zn²⁺ cation.