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TitleNovel multidomain, multifunctional glycoside hydrolases from highly lignocellulolytic Caldicellulosiruptor species
Journal, issue, pagesAIChE J., Year 2019
Publish dateApr 19, 2018 (structure data deposition date)
AuthorsConway, J.M. / Crosby, J.R. / Hren, A.P. / Southerland, R.T. / Lee, L.L. / Lunin, V.V. / Alahuhta, P.M. / Himmel, M.E. / Bomble, Y.J. / Adams, M.W.W. / Kelly, R.M.
External linksAIChE J. / Search PubMed
MethodsX-ray diffraction
Resolution1.9 - 2 Å
Structure data

PDB-6d5b:
Structure of Caldicellulosiruptor danielii CBM3 module of glycoside hydrolase WP_045175321
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6d5c:
Structure of Caldicellulosiruptor danielii GH10 module of glycoside hydrolase WP_045175321
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6d5d:
Structure of Caldicellulosiruptor danielii GH48 module of glycoside hydrolase WP_045175321
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-FMT:
FORMIC ACID

Source
  • caldicellulosiruptor sp. wai35.b1 (bacteria)
KeywordsSUGAR BINDING PROTEIN / CBM3 / carbohydrate binding / HYDROLASE / GH10 / glycoside hydrolase / GH48

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