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. 2015 Aug 20;15:15. doi: 10.1186/s12900-015-0042-4

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© Yang et al. 2015

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 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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Fig. 6 — Potential functional cavity of SpCBM. a The surface electrostatic view from the top of the binding site of SpCBM and a cavity adjacent to the active site, which is occupied by a lysine from a symmetry related molecule (shown in cyan). b Close-up view of the interaction between the lysine and the protein. The solvent-accessible surface of SpCBM is coloured based on the electrostatic potential from −7 (red) to +7 (blue) kT/e, calculated using the APBS tool in PyMOL [34, 35]