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. 2018 Oct 4;8:14796. doi: 10.1038/s41598-018-32967-1

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© The Author(s) 2018

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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PmMOR^V150M progesterone binding. (A) Stereo-view of the active site of PmMOR^V150M in complex with NADP⁺ and progesterone with protein and side chains shown in gray. Selected residues near the ligand are shown in sticks. NADP⁺ is colored by atom with carbons in gray. Progesterone is colored by atom with carbons in cyan. The binding mode of progesterone postulated by Thorn, et al.²⁴ is shown and colored by atom with carbons in gray. Note the steric clash with ASN-205 for this binding mode. Distances between the reactive hydride and carbon-carbon double bond to be reduced are 6.3 Å and 7.1 Å for the PmMOR and Thorn, et al. conformation, respectively. (B) PmMOR^V150M progesterone omit map contoured at +3.5 standard deviations (σ) above the mean shown in green mesh. Selected side chain residues are drawn as sticks and labeled. The PmMOR^WT progesterone ligand is shown in yellow sticks and the PmMOR^V150M progesterone is shown in cyan sticks.