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![[Figure 3]](ud5029fig3mag.jpg)
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Figure 3
Active-site architecture of SoBDH2. Residues of the catalytic motif are colored orange and residues of SoBDH2 lining the active site are colored light green. The substrate-binding pocket is completed by Leu277 (underlined) from the other, neighboring protomer. (a) Substrate-binding pocket of SoBDH2. Numbering refers to residues of SoBDH2. (b) Superposition of the cryoEM structure of SoBDH2 and the crystal structure of SrBDH1–NAD+ (PDB entry 6zyz; Chánique et al., 2021  ). Residues of SrBDH1 are drawn in light blue or marine for Phe260 (underlined) from the other, neighboring protomer. The numbering of amino acids refers to SrBDH1. Residues in the equivalent positions to Ile196 and Val197 in SrBDH1–NAD+ are not resolved in the density of SoBDH2 due to the absence of NAD+. The corresponding residues to the latter two residues in SoBDH2 are Leu206 and Ala207, respectively. The yellow ellipse indicates the potential substrate-binding site. |
![[Figure 3]](ud5029fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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