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. 2021 Nov 24;11:22849. doi: 10.1038/s41598-021-02180-8

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© The Author(s) 2021

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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Superposition of Nmar_1308 with homologous structures. Superposition is performed by using cryo-synchrotron structure of Nmar_1308 with published apo/ligand bound structures of enoyl-CoA hydrates and 3-hydroxypropionyl-CoA dehydratase (3HPD). Average RMSD values were calculated from all pairwise RMSD values between Cα atoms of an Nmar_1308 monomer and one of the superimposed monomers of homologous enzymes (36 pairs for hexamers and 18 for trimers), and are indicated below each panel. All standard errors of the RMSDs are below 0.01 Å. Chain A of Nmar_1308 is colored in pale green while the superposed structure is colored in gray. The ligands were represented with arrows. The figure is generated by PyMOL (www.schrodinger.com/pymol). (HXC: hexanoyl-CoA, CAA: acetoacetyl-CoA, CO8: octanoyl-CoA, DAK: 4-(N,N-dimethylamino)cinnamoyl-CoA, COA: coenzyme A).