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. 2019 Mar 20;9:4905. doi: 10.1038/s41598-019-41355-2

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© The Author(s) 2019

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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Molecular modeling of GAG in complex with proMMP2. Docking results using Autodock3 and DBSCAN clustering are shown. proMMP2 (PDB ID 1GXD (3.1 Å)) is shown in cartoon and colored by domains: propeptide (light pink), catalytic domain (pale), FNII (green) and PEX domain (grey). Different clusters of GAG are shown in sticks with gradient colors: (A) C4S (green), (B) C6S (green), (C) HA (brown), (D) SH (pink) and (E) HE (teal). Calcium and zinc ions are shown in green and grey spheres, respectively. The TIMP3 model, although not taken into account for docking calculations, is shown in blue transparency just for illustrative purposes. Discontinuous black circles and rectangles highlight the PEX domain recognition by TIMP3 C-terminal tail and FNII, respectively.