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Structure paper

TitleStructures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis.
Journal, issue, pagesBiochemistry, Vol. 51, Page 6816-6826, Year 2012
Publish dateMar 18, 2014 (structure data deposition date)
AuthorsNomme, J. / Su, Y. / Konrad, M. / Lavie, A.
External linksBiochemistry / PubMed:22861376
MethodsX-ray diffraction
Resolution1.75 - 2.13 Å
Structure data

PDB-4pvp:
Crystal structure of malonate-bound human L-asparaginase protein
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-4pvq:
Crystal structure of sulfate-bound human l-asparaginase protein
Method: X-RAY DIFFRACTION / Resolution: 2.13 Å

PDB-4pvr:
Crystal structure of partially-cleaved human l-asparaginase protein in complex with l-aspartate
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-4pvs:
Crystal structure of fully-cleaved human l-asparaginase protein in complex with l-aspartate
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

Chemicals

ChemComp-MLI:
MALONATE ION

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-IOD:
IODIDE ION

ChemComp-ASP:
ASPARTIC ACID

Source
  • homo sapiens (human)
KeywordsHYDROLASE / NTN ENZYME / HOMODIMER / L-ASPARAGINE

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