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. Author manuscript; available in PMC: 2020 Feb 1.
Published in final edited form as: J Mol Biol. 2018 Dec 7;431(3):524–541. doi: 10.1016/j.jmb.2018.11.030

Fig. 3.

Fig. 3.

Crystal structure of LsALDH16. (A) Structure of the protomer, highlighting secondary structure and domain architecture. NADH is shown in pink sticks. (B) Surface representation of the LsALDH16 protomer. (C) Superposition of the LsALDH16 protomer with a dimer of ALDH2 showing trans-hierarchical structural symmetry. The coloring of the LsALDH16 domains is the same as in panel A. The color of the ALDH2 domains is the same as in Fig. 1. Note that LsALDH16 is structurally equivalent to three-fourths of a classical ALDH dimer.