Fig. 2: Structural comparison of FLO7 and HglS.
From: An iron (II) dependent oxygenase performs the last missing step of plant lysine catabolism
a FLO7 crystal structure displayed as cartoon sheets and helices. Metal-coordinating and substrate-binding residues are shown as sticks, while the 2-oxoadipate substrate is shown as green sticks. The nickel bound within the active site is shown as a tan sphere. b Overlay of HglS (teal) and FLO7 (yellow) structures showing metal-coordinating residues, substrate-binding residues, the active site metal, and the 2-oxoadipate substrate. Right inset: HglS (teal) and FLO7 (yellow) active sites displaying conserved residues and substrate-binding mode. The 2OA substrates are colored light blue (HglS) and white (FLO7), and the active site bound nickel shown as spheres and colored blue (HglS) and olive (FLO7).
