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. 2022 Aug 30;12:14737. doi: 10.1038/s41598-022-19040-8

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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 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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Model of the coenzyme binding site highlighting the conservation of putative coenzyme binding residues. (A) NADP⁺ was modeled by superimposing the ternary complex of AKR6A2 with apo-DepB_Rleg. White sticks represent the residues from DepB_Rleg complex, while cyan sticks are residues corresponding to AKR6A2. Trp-206 has been re-oriented in the apo-DepB_Rleg structure to prevent a steric clash with the nicotinamide ring of NADP⁺. π-stacking interactions between the nicotinamide ring and Trp-206 are shaded in blue. In apo-DepB_Rleg, Lys-217 points away from the entrance of the coenzyme binding pocket. However, by analogy to Lys-254 in AKR6A2, this residue may interact with at least one of the oxygen atoms of 2’monophosphate. (B) MSA depicting conservation of residues near the 2’monophosphate of the modeled NADP⁺ (See Supplementary Table S1 for accession codes).