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. 2015 Jan 28;16:28. doi: 10.1186/s12859-015-0465-8

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© Kulik et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Docking of C-6 modified substrates. A. Overlay of the active sites of TfHex with docked pNP-GlcNAc (2; vivid color, yellow hydrogen bonds) and pNP-GlcNAc-sulfate (6; grey). Sodium ion in the active site with the sulfated substrate is shown. B. TfHex active site with sulfated substrate 6 in the active site. Sodium ion penetrated in the active site from water solution is shown by yellow ball. Negatively charged amino acids close to the sulfo-group are shown and labeled. Distance from Cδ atom of Glu 332 and Glu 546 to sulfur atom of substrate is 0.537-0.602 and 0.465-0.609 nm, respectively, from Cε atom of Asp 472 to sulfur atom of substrate it is 0.619-0.819 nm. C. Overlay of the active site of S. plicatus hexosaminidase with docked sulfated compound (6; vivid color) and pNP-GlcNAc (2; grey). D. Overlay of the active site of S. plicatus hexosaminidase with docked pNP-GlcNAc-uronate (5; vivid) and pNP-GlcNAc (2; grey).