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. 2022 Sep 19;13:5485. doi: 10.1038/s41467-022-32993-8

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — a Solvent accessible surface representation of V-Csn apo1 structure with four conserved acidic residues (yellow and red sticks) clustering within the inter-domain cleft. Surface colored as for Fig. 2d: Domain-1, green; Domain-2, pink. b Close-up of putative active site highlighting the four conserved acidic residues. Hydrogen bonds shown as dashed black lines and water molecules as red spheres. c Electrostatic surface of V-Csn apo1 calculated at pH 4.6. Surface is contoured from −5 kT/e (red) to +5 kT/e (blue). d Electrostatic surface of V-Csn apo1 calculated at pH 5.5. Surface is contoured from −5 kT/e (red) to +5 kT/e (blue). e Solvent accessible surface representation of chitohexaose-V-Csn complex showing location of trisaccharide moiety (yellow, blue and red CPK spheres) in active site cleft. Orientation of molecule in top view is approximately the same as in a, and bottom view is rotated 90° to show side view. Enzyme colored by structural domains (Domain-1, green; Domain-2, pink). f Residual F_o-F_c electron density (pink mesh) for bound substrate contoured at 2.5 σ. Electron density map was calculated following molecular replacement and prior to the incorporation of substrate. Final refined trisaccharide molecule (GlcN-1, GlcN-2 and GlcN-3) is shown as cyan sticks. g Ribbon representation of chitohexaose-V-Csn complex with trisaccharide (cyan sticks) bound in the active site. Hydrogen bonds indicated by dashed black lines and water molecules as small red spheres (Domain-1, green; Domain-2, pink). h Solvent accessible surface representation of cellohexaose complex of Humicola isolens endoglucanase V (Cel45): DPBB domain, yellow; two loops for small sub-domains, brown (lower) and orange (upper). Cellohexaose molecule (magenta) is bound in narrow tunnel between DPBB domain and the two loops. View on right side of panel is rotated 90° to show the tunnel-like active site, in contrast to the open active site in V-Csn. i Solvent accessible surface representation of Cryptopygus antarcticus endoglucanase CaCel: DPBB domain, light blue; two loops are colored blue (lower) and cyan (upper). Location of substrate bonding cleft and tunnel indicated by cellohexaose molecule (magenta sticks) derived from the Cel45 complex in h.