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Structure paper

TitleStructures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 24, Page 362-369, Year 2017
Publish dateOct 6, 2016 (structure data deposition date)
AuthorsLi, B. / Li, H. / Lu, L. / Jiang, J.
External linksNat. Struct. Mol. Biol. / PubMed:28319083
MethodsX-ray diffraction
Resolution2.13 - 2.5 Å
Structure data

PDB-5tke:
Crystal Structure of Eukaryotic Hydrolase
Method: X-RAY DIFFRACTION / Resolution: 2.481 Å

PDB-5un8:
Crystal Structure of human O-GlcNAcase in complex with glycopeptide p53
Method: X-RAY DIFFRACTION / Resolution: 2.13 Å

PDB-5un9:
The crystal structure of human O-GlcNAcase in complex with Thiamet-G
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-NHT:
(3AR,5R,6S,7R,7AR)-2-(ETHYLAMINO)-5-(HYDROXYMETHYL)-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL

Source
  • homo sapiens (human)
KeywordsHYDROLASE / human O-GlcNAcase; glycopeptide / Human O-GlcNAcase / Thiemat-G

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