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TitleThe Catalytic Acid-Base in GH109 Resides in a Conserved GGHGG Loop and Allows for Comparable alpha-Retaining and beta-Inverting Activity in an N-Acetylgalactosaminidase from Akkermansia muciniphila
Journal, issue, pagesAcs Catalysis, Year 2020
Publish dateOct 8, 2019 (structure data deposition date)
AuthorsTeze, D. / Shuoker, B. / Chaberski, E.K. / Kunstmann, S. / Fredslund, F. / Nielsen, T.S. / Stender, E.G.P. / Peters, G.H.J. / Nordberg Karlsson, E. / Welner, D.H. / Abou Hachem, M.
External linksAcs Catalysis / Search PubMed
MethodsX-ray diffraction
Resolution2.13 Å
Structure data

PDB-6t2b:
Glycoside hydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+.
Method: X-RAY DIFFRACTION / Resolution: 2.13 Å

Chemicals

ChemComp-A2G:
2-acetamido-2-deoxy-alpha-D-galactopyranose

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • akkermansia muciniphila (bacteria)
KeywordsHYDROLASE / Glycoside hydrolase / inverting / retaining

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