2vi0 | pdb_00002vi0

Lichenase CtLic26 in complex with a thio-oligosaccharide

spinqualitylabelsall models 2vi0, resolution 1.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vi0 is a 1 chain structure with sequence from Acetivibrio thermocellus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.51Å Ligands: BGC, MGL, PRD_900005, SGC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GUNH_ACET2 This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The substrate binding regions of a beta-1,3:1,4 glucanase are revealed through structural analysis with a thio-oligosaccharide and kinetics of enzyme variants. Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants.,Money VA, Cartmell A, Guerreiro CI, Ducros VM, Fontes CM, Gilbert HJ, Davies GJ Org Biomol Chem. 2008 Mar 7;6(5):851-3. Epub 2008 Feb 4. PMID:18292875 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase 3D structures

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