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TitleCrystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH.
Journal, issue, pagesProtein Eng., Vol. 11, Page 1121-1128, Year 1998
Publish dateJul 14, 1998 (structure data deposition date)
AuthorsFushinobu, S. / Ito, K. / Konno, M. / Wakagi, T. / Matsuzawa, H.
External linksProtein Eng. / PubMed:9930661
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-1bk1:
ENDO-1,4-BETA-XYLANASE C
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • aspergillus kawachii (mold)
KeywordsHYDROLASE / XYLAN DEGRADATION / GLYCOSIDASE

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