Extended Data Fig. 4: HDO structural comparison of substrate binding site and diiron cofactor sites.
From: A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile
a, Diiron site and substrate binding sites of AetD reproduced here from Fig. 3A. Substrate shown with green carbons. b, Diiron site and substrate binding sites of UndA25 (PDB ID: 6P5Q) are similar to those of AetD. In both structures, the substrate is stabilized by hydrophobic interactions at enzyme core. AetD substrate binds Fe1 in a bidentate manner whereas UndA binds Fe1 only through one of the oxygen atoms in its carboxylate moiety. c, Diiron site and putative substrate binding site of HDO enzyme SznF27 (PDB ID: 6VZY). Note: no substrate-bound structure is available for SznF; the dashed line in the bottom panel indicates the expected substrate binding position.
