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![[Figure 3]](dw5211fig3mag.jpg)
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Figure 3
Active site and conformational itinerary of MgGH51. (a) Active-site arrangement of MgGH51 around α-L-arabinofuranose. Active-site residues interacting with α-L-arabinofuranose (brown) are shown as blue sticks. Apparent hydrogen-bonding interactions are shown as black dashed lines. The interaction between the catalytic nucleophile and the anomeric C atom is shown as an orange dashed line. Electron density is shown as a mesh contoured at 1.5σ. (b) Overlay of the AraDNJ and α-L-AraAZI ligands within the MgGH51 active site. The active-site residues and ligand from the α-L-AraAZI complex are shown as grey sticks. The active-site residues and ligand from the AraDNJ complex are shown as cyan sticks. Apparent hydrogen-bonding interactions are shown as black dashes. |
![[Figure 3]](dw5211fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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