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Structure paper

TitleStructural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 35675-35684, Year 2010
Publish dateDec 13, 2007 (structure data deposition date)
AuthorsLitzinger, S. / Fischer, S. / Polzer, P. / Diederichs, K. / Welte, W. / Mayer, C.
External linksJ. Biol. Chem. / PubMed:20826810
MethodsX-ray diffraction
Resolution1.4 - 1.836 Å
Structure data

PDB-3bmx:
Beta-N-hexosaminidase (YbbD) from Bacillus subtilis
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-3nvd:
Structure of YBBD in complex with pugnac
Method: X-RAY DIFFRACTION / Resolution: 1.836 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-NA:
Unknown entry

ChemComp-P4G:
1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE

ChemComp-HOH:
WATER

ChemComp-OAN:
O-(2-ACETAMIDO-2-DEOXY D-GLUCOPYRANOSYLIDENE) AMINO-N-PHENYLCARBAMATE / inhibitor*YM

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

Source
  • bacillus subtilis (bacteria)
KeywordsHYDROLASE / beta-N-hexosaminidase / Bacillus subtilis / TIM barrel / Glycosidase / Lipoprotein / Membrane / Palmitate

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