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. 2022 May 13;5:459. doi: 10.1038/s42003-022-03384-y

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© The Author(s) 2022

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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Fig. 3 — a EcDHFR:TMP (green), b EcDHFR:TMP:NADPH (magenta), c DfrA1:TMP (light blue), and d DfrA5:TMP:NADPH (beige). e Overlays of the crystal structures of DHFR with TMP ternary complexes; EcDHFR:TMP:NADPH (magenta) superimposed onto DfrA5:TMP:NADPH (beige), f Binary complexes; EcDHFR:TMP (green) superimposed onto DfrA1:TMP (light blue), g DfrA1:TMP (light blue) and DfrA5:TMP:NADPH (beige), and h DfrA5:TMP:NADPH (beige) superimposed onto Human DHFR:TMP:NADPH (PDB id code 2W3A). Residues important to ligand binding are shown in stick mode and colored by atom.