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Structure paper

TitleL-asparaginase from Escherichia coli: Novel insights about the behavior of flexible part of the active site
Journal, issue, pagesTo Be Published
Publish dateDec 4, 2019 (structure data deposition date)
AuthorsSouza, T.A.C.B. / Morais, S.B. / Morini, F.S. / Meissner, G.O.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.83 - 2.1 Å
Structure data

PDB-6v5f:
L-asparaginase from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-7m11:
L-asparaginase from Escherichia coli with bound Aspartic acid
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

Chemicals

ChemComp-ASP:
ASPARTIC ACID

ChemComp-SIN:
SUCCINIC ACID

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / L-asparaginase / catalytic mechanism / leukemia

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