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Fig. 4 | Biotechnology for Biofuels

Fig. 4

From: Structural and functional characterization of a highly stable endo-β-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst

Fig. 4

Overall structure of unliganded F. oxysporum Xyl2. a Ribbon representation of the unliganded Xyl2 crystal structure at 1.56 Å resolution with annotated secondary structure elements. The N- and C-termini are labeled. Helix 310A and α1 are colored in cyan, β-strands in pink, and interconnecting loops and the extremes are shown in salmon. The orientation shown provides a view into the wide and elongated active-site groove, which was filled with water and solvent molecules in the crystal structure. b Overall ribbon structure of Xyl2 (in cyan) showing residues thought to interact with the cognate xylan substrate are shown as sticks in the electron density map (contoured at 1σ level). Compared with the orientation shown in a, this orientation is slightly rotated clockwise around a vertical axis

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