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Structure paper

TitleStructural and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis.
Journal, issue, pagesProtein Sci., Vol. 26, Page 985-996, Year 2017
Publish dateNov 30, 2016 (structure data deposition date)
AuthorsSingh, R.K. / Steyaert, J. / Versees, W.
External linksProtein Sci. / PubMed:28218438
MethodsX-ray diffraction
Resolution1.65 Å
Structure data

PDB-5mj7:
Structure of the C. elegans nucleoside hydrolase
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HOH:
WATER

Source
  • caenorhabditis elegans (invertebrata)
KeywordsHYDROLASE / nucleoside hydrolase / N-ribohydrolase / leaving group activation / enzyme mechanism

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