Structural insight into the hydrolase and synthase activities of an alkaline α-galactosidase from Arabidopsis from complexes with substrate/product

Chuankhayan, P.; Lee, R.-H.; Guan, H.-H.; Lin, C.-C.; Chen, N.-C.; Huang, Y.-C.; Yoshimura, M.; Nakagawa, A.; Chen, C.-J.

doi:10.1107/S2059798323000037

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 5
The active-site structure of D383A in complex with stachyose. The complexed structure reveals the complete subsites (–1, +1, +2 and +3) in the catalytic binding site of AtAkαGal3. The glucose in the +2 subsite, stabilized by Arg451, Tyr215 and Trp211 through water-mediated hydrogen-bond interactions, is located nearly at the edge of the pocket cavity. The binding interaction of fructose in the +3 subsite, which is located at the outer edge of the cavity, is utilized only by Asp346 (magenta sticks) and one water molecule at the outer edge of the cavity. Stachyose, protein residues and water molecules are shown as yellow sticks, green sticks and cyan spheres, respectively.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 79| Part 2| February 2023| Pages 154-167

https://doi.org/10.1107/S2059798323000037

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