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Figure 4
The mode of binding of compound 7 (3,4-di­meth­oxy­phenyl­acetamide) in the wider substrate specificity pocket of the DA1472 variant. (a) Shown are the substrate analog of 3,4-di­meth­oxy­phenyl­acetamide (gray, E9I), as well as the Fe2+ ion, ADPR and the residues Gly151 and Val259 (PDB entry 7qls). Superimposed are NAD+ and the residues Asn151 and Leu259 of the wild-type active site (PDB entry 5br4). Also shown is the superimposed ethyl­eneglycol (EDO, cyan) as observed in the DA1472 variant (PDB entry 7qnf) and interacting with the Fe2+ ion (dotted line). `H' identifies the N-terminal end of the pyrophosphate-binding helix of the NAD-binding domain (brown). The Fe2+-binding domain is colored green. (b) Zoomed-in view of the substrate-binding pocket with bound 3,4-di­meth­oxy­phenyl­acetamide, visualizing the extra space generated by the N151G and the L259V amino acid changes. Gly151 (yellow) and Val259 (yellow) are of the DA1472 variant of the structure with bound 3,4-di­meth­oxy­phenyl­acetamide (gray, E9I) (PDB entry 7qls). Superimposed are Asn151 (orange) and Leu259 (green) of the wild-type active site (PDB entry 5br4), which are also represented by their molecular surfaces.

IUCrJ
Volume 10| Part 4| July 2023| Pages 437-447
ISSN: 2052-2525
https://doi.org/10.1107/S205225252300444X