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Structure paper

TitleContribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora Viridifaciens
Journal, issue, pagesFEBS Lett., Vol. 577, Page 265-, Year 2004
Publish dateSep 24, 2004 (structure data deposition date)
AuthorsWatson, J.N. / Newstead, S. / Dookhun, V. / Taylor, G. / Bennet, A.J.
External linksFEBS Lett. / PubMed:15527797
MethodsX-ray diffraction
Resolution1.7 - 2.1 Å
Structure data

PDB-1w8n:
Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens.
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1w8o:
Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-GAL:
beta-D-galactopyranose

ChemComp-DAN:
2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CIT:
CITRIC ACID

ChemComp-GOL:
GLYCEROL

Source
  • micromonospora viridifaciens (bacteria)
KeywordsHYDROLASE / GLYCOSIDASE / NEURAMINIDASE / BETA- PROPELLER FOLD. / SIALIDASE / BETA-PROPELLER

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