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TitleChaetomella raphigerabeta-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis.
Journal, issue, pagesBiotechnol Biofuels, Vol. 12, Page 258-258, Year 2019
Publish dateApr 23, 2019 (structure data deposition date)
AuthorsKao, M.R. / Kuo, H.W. / Lee, C.C. / Huang, K.Y. / Huang, T.Y. / Li, C.W. / Chen, C.W. / Wang, A.H.J. / Yu, S.M. / Ho, T.H.D.
External linksBiotechnol Biofuels / PubMed:31700541
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-6jxg:
Crystasl Structure of Beta-glucosidase D2-BGL from Chaetomella Raphigera
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-HOH:
WATER

Source
  • chaetomella raphigera (fungus)
KeywordsHYDROLASE / glucosidase / glycoside hydrolase

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