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. 2020 Mar 27;10:5656. doi: 10.1038/s41598-020-62548-0

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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 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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Comparison of free PGM1-2 and substrate and product complexes. (a) Structural alignment of PGM1-2 with no bound ligand (grey) and the complexes PGM1-2:G1P (pale pink) and PGM1-2:G6P (light cyan), rendered as a Cα trace, shows that ligand binding does not affect overall structure. Ligands are shown in sticks representation, phosphoserine (p-Ser135) as ball-and-sticks, and the active site divalent cation as a sphere (grey). (b) Active site region magnified, with coloring and rendering as in panel (a) (rotated roughly 90° out of the plane). (c) Polder OMIT map for G1P in the PGM1-2:G1P complex contoured at 4.0σ strongly supports the presence of the ligand (sticks rendering) in the crystal structure. Selected active site residues, p-Ser135, phosphate-binding Arg521 and Arg533, as well as Asp306, Asp308, and Asp310 complexing the divalent cation (grey sphere), are shown as ball-and-sticks. (d) Polder OMIT map for G6P in the PGM1-2:G6P complex contoured at 3.5σ.