Extended Data Fig. 3: Heme- and FAD-binding sites.
From: Structures of mouse DUOX1–DUOXA1 provide mechanistic insights into enzyme activation and regulation
a, Structural comparison of heme-binding sites between DUOX1 (blue) and csNOX5 (gray). The transmembrane helices are labeled with S1–S6. b, Structural conservation of heme coordination in ferric oxidoreductases. DUOX1, csNOX5, Cyto b561 and Dcytb are colored in blue, gray, light blue and cyan, respectively. c, FAD-binding site in 2D representation. Hydrogen bonds, hydrophobic interactions and cation-π interactions are indicated by dashes, spokes and vertical dashes, respectively. Residues from FBD, NBD, TMD are colored in light pink, gray and blue, respectively. d, The putative oxygen-binding site. Oxygen is represented by a dashed red oval. e, The possible oxygen entering and hydrogen peroxide exiting paths.
