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Structure paper

TitleDo bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu?
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1550, Page 117-128, Year 2001
Publish dateAug 17, 2001 (structure data deposition date)
AuthorsAghaiypour, K. / Wlodawer, A. / Lubkowski, J.
External linksBiochim. Biophys. Acta / PubMed:11755201
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-1jsl:
Crystal structure of Erwinia chrysanthemi L-asparaginase complexed with 6-HYDROXY-D-NORLEUCINE
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1jsr:
CRYSTAL STRUCTURE OF ERWINIA CHRYSANTHEMI L-ASPARAGINASE COMPLEXED WITH 6-HYDROXY-L-NORLEUCINE
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-DDO:
6-HYDROXY-D-NORLEUCINE

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-LDO:
6-HYDROXY-L-NORLEUCINE

Source
  • erwinia chrysanthemi (bacteria)
KeywordsHYDROLASE / L-asparaginase / amidohydrolase / bacteria / covalent complex / suicide inhibitor / DON / enzyme / active site / tetramer / ASPARAGINASE / 6-DIAZO-5-OXO-L-NORLEUCINE

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