Extended Data Fig. 6: Comparison of the active site access between SN243 and the structure of a homologous GH3 member.
From: Functional metagenomic screening identifies an unexpected β-glucuronidase
(a) Cartoon representation of the structures of SN243 (crystal structure with density for loop His190-Ala202, PDB: 7QG4, green) and Saccharopolyspora erythraea glucan β-1,4-glucosidase (PDB: 5M6G, blue). (b) The zoom into the active site with the reaction product GlcA (yellow) shows loops folding over the binding pocket in the glucan β-1,4-glucosidase (blue), making the active site much smaller than in SN243 (green). (c) Surface display of SN243 (green) and the glucan β-1,4-glucosidase (blue). Active site binding pockets have been calculated by Castp 3.0 and are highlighted. The active site volume of SN243 is with 1293 Å3 about twenty times as large as the active site volume (65 Å3) of the homologous GH3 structure.
