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Structure paper

TitleElucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate Hydrolysis.
Journal, issue, pagesJ. Mol. Biol., Vol. 426, Page 2471-2485, Year 2014
Publish dateDec 13, 2013 (structure data deposition date)
AuthorsNomme, J. / Su, Y. / Lavie, A.
External linksJ. Mol. Biol. / PubMed:24768817
MethodsX-ray diffraction
Resolution1.5 - 2.1 Å
Structure data

PDB-4o0c:
High resolution crystal structure of uncleaved human L-asparaginase protein
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-4o0d:
Crystal structure of the human L-asparaginase protein T168S mutant
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-4o0e:
Crystal structure of the human L-asparaginase protein T186V mutant
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

PDB-4o0f:
Crystal structure of the human L-asparaginase protein T219A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

PDB-4o0g:
Crystal structure of the human L-asparaginase protein T219V mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4o0h:
Crystal structure of human L-asparaginase protein with covalently linked substrate L-asparagine
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GLY:
GLYCINE

ChemComp-IAS:
BETA-L-ASPARTIC ACID

Source
  • homo sapiens (human)
KeywordsHYDROLASE / NTN ENZYME / HOMODIMER / Asparaginase

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