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Figure 2
(a) Structure of the AdRedAm dimer from data set 1 in ribbon format, with monomers A and B shown in blue and brown, respectively. (b) Active site of AdRedAm showing the active-site residues, each of which is conserved from AspRedAm (PDB entry 5g6r; Aleku et al., 2017BB4). NADPH4 is shown in cylinder format with C atoms in grey. (c) Superimposition of monomers E and I of AdRedAm from data set 2 in blue and brown, respectively. (d) Structure of AdRedAm from data set 3. The symmetry neighbour has been incorporated (C atoms in brown) to show the contribution of both monomers in the active site. The ligand 2,2-difluoroacetophenone (15) is shown with C atoms in yellow. Electron density in blue corresponds to the unbiased FoFc maps at a level of 2.5σ obtained before refinement of the ligand atoms, which have been added for clarity.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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