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. 2020 Nov 26;10:20615. doi: 10.1038/s41598-020-77699-3

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© The Author(s) 2020

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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MMP1 structure (PDB ID: ISU3). The hemopexin domain is connected to the catalytic domain by a flexible linker. The pro domain is cleaved off to activate MMPs for catalysis. Yellow and purple spheres represent the van der Waals radii of the calcium and zinc atoms, respectively. The pro domain, the catalytic domain, the linker, and the hemopexin domains are roughly defined by the ranges of residues D32-Q99, F100-Y260, G261-C278, and D279-C466, respectively.