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Structure paper

TitleStructural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolases.
Journal, issue, pagesPlant Cell, Vol. 14, Page 1033-1052, Year 2002
Publish dateMay 22, 2001 (structure data deposition date)
AuthorsHrmova, M. / De Gori, R. / Smith, B.J. / Fairweather, J.K. / Driguez, H. / Varghese, J.N. / Fincher, G.B.
External linksPlant Cell / PubMed:12034895
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-1j8v:
Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-LAM:
4'-NITROPHENYL-S-(BETA-D-GLUCOPYRANOSYL)-(1-3)-(3-THIO-BETA-D-GLUCOPYRANOSYL)-(1-3)-BETA-D-GLUCOPYRANOSIDE

ChemComp-HOH:
WATER

Source
  • hordeum vulgare (barley)
KeywordsHYDROLASE / 2-domain fold / ligand-protein complex

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