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. 2022 Aug 17;12:14010. doi: 10.1038/s41598-022-17384-9

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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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NADP binding in P. aeruginosa (5BNT), H. influenzae (1PQU) and V. cholerae (3PZR) ASADH proteins. (A) Schematic of hydrogen bonds (H-bond) between bonding residues of P. aeruginosa ASADH and NADP. (B) NADP (yellow) bound within the P. aeruginosa ASADH dimer and active site residues within the NADP binding site cavity that are important for H-bonding (green). (C) Residues responsible for NADP H-bonding in P. aeruginosa (5BNT, purple), H. influenzae (1PQU, blue) and V. cholerae (3PZR, green) show several conserved residues in NADP binding. (D) Superimposed structures of P. aeruginosa (5BNT, purple), H. influenzae (1PQU, blue) and V. cholerae (3PZR, green) showing the binding surface of the ASADH proteins (grey) modelled in SeeSAR Version 9.2⁴².