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Structure paper

TitleUnusual active site location and catalytic apparatus in a glycoside hydrolase family.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 114, Page 4936-4941, Year 2017
Publish dateJan 13, 2017 (structure data deposition date)
AuthorsMunoz-Munoz, J. / Cartmell, A. / Terrapon, N. / Henrissat, B. / Gilbert, H.J.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:28396425
MethodsX-ray diffraction
Resolution1.39 - 1.8 Å
Structure data

PDB-5muk:
Glycoside Hydrolase BT3686
Method: X-RAY DIFFRACTION / Resolution: 1.49 Å

PDB-5mul:
Glycoside Hydrolase BT3686 bound to Glucuronic Acid
Method: X-RAY DIFFRACTION / Resolution: 1.39 Å

PDB-5mum:
Glycoside Hydrolase BACINT_00347
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5mvh:
Glycoside Hydrolase BACCELL_00856
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-BDP:
beta-D-glucopyranuronic acid

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

Source
  • bacteroides thetaiotaomicron (strain atcc 29148 / dsm 2079 / nctc 10582 / e50 / vpi-5482) (bacteria)
  • bacteroides intestinalis dsm 17393 (bacteria)
  • bacteroides cellulosilyticus dsm 14838 (bacteria)
KeywordsHYDROLASE / Rhamnosidase / Bacteroides / Beta-propeller

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