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TitleThe accessory domain changes the accessibility and molecular topography of the catalytic interface in monomeric GH39 beta-xylosidases.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 68, Page 1339-1345, Year 2012
Publish dateApr 9, 2012 (structure data deposition date)
AuthorsSantos, C.R. / Polo, C.C. / Correa, J.M. / Simao, R.C. / Seixas, F.A. / Murakami, M.T.
External linksActa Crystallogr. ,Sect. D / PubMed:22993088
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-4ekj:
Crystal structure of a monomeric beta-xylosidase from Caulobacter crescentus CB15
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • caulobacter vibrioides (bacteria)
KeywordsHYDROLASE / TIM-barrel fold / hemicellulase

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