ZmALDH2B2/RF2A structural surface and pocket/cavity element analysis. (A) The surface conformation of ZmALDH2B2/RF2A is depicted showing the secondary structure elements inside. The morphology of the cavity accommodating NAD(P)+ cofactor is represented in high magnification. Detail view organization of the predicted amino acids of the pocket is represented in blue color. The space-filled representation of van der Waals surface of the cofactor, and the catalytic amino acid residues Cys 312 (green) and Glu 278 (red) that interact with the aldehyde substrate and drive the MAD(P)+ cofactor dependent reaction is depicted. (B) Cavity and pocket analysis of ZmALDH2B2/RF2A shows nine pockets, and a big tunnel made of two continuous pockets with a total volume of 1292Å3. A detailed view of the cofactor binding pocket and the big tunnel in the opposite side of the structure is shown.