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6XUT

Crystallographic structure of oligosaccharide dehydrogenase from Pycnoporus cinnabarinus, ligand-free form

Summary for 6XUT
Entry DOI10.2210/pdb6xut/pdb
DescriptorOligosaccharide dehydrogenase, beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
Functional Keywordsglucose dehydrogenase, pycnoporus cinnabarinus, oxidoreductase, oligosaccharide dehydrogenase
Biological sourcePycnoporus cinnabarinus (Cinnabar-red polypore)
Total number of polymer chains1
Total formula weight65671.00
Authors
Cerutti, G.,Savino, C.,Montemiglio, L.C.,Sciara, G.,Vallone, B. (deposition date: 2020-01-21, release date: 2021-02-03, Last modification date: 2024-10-16)
Primary citationCerutti, G.,Gugole, E.,Montemiglio, L.C.,Turbe-Doan, A.,Chena, D.,Navarro, D.,Lomascolo, A.,Piumi, F.,Exertier, C.,Freda, I.,Vallone, B.,Record, E.,Savino, C.,Sciara, G.
Crystal structure and functional characterization of an oligosaccharide dehydrogenase from Pycnoporus cinnabarinus provides insights into fungal breakdown of lignocellulose.
Biotechnol Biofuels, 14:161-161, 2021
Cited by
PubMed Abstract: Fungal glucose dehydrogenases (GDHs) are FAD-dependent enzymes belonging to the glucose-methanol-choline oxidoreductase superfamily. These enzymes are classified in the "Auxiliary Activity" family 3 (AA3) of the Carbohydrate-Active enZymes database, and more specifically in subfamily AA3_2, that also includes the closely related flavoenzymes aryl-alcohol oxidase and glucose 1-oxidase. Based on sequence similarity to known fungal GDHs, an AA3_2 enzyme active on glucose was identified in the genome of Pycnoporus cinnabarinus, a model Basidiomycete able to completely degrade lignin.
PubMed: 34294139
DOI: 10.1186/s13068-021-02003-y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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