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X-ray diffraction
1.7Å resolution

Function and Biology Details

Reaction catalysed: 
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156164 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-asparaginase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 330 amino acids
Theoretical weight: 34.9 KDa
Source organism: Wolinella succinogenes DSM 1740
Expression system: Escherichia coli
UniProt:
  • Canonical: P50286 (Residues: 1-330; Coverage: 100%)
Gene names: WS0660, ansA, ansB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ASP 4 x ASP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 144.755Å b: 71.459Å c: 141.502Å
α: 90° β: 118.07° γ: 90°
R-values:
R R work R free
0.177 0.175 0.207
Expression system: Escherichia coli

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Citations

4 review citations

What makes a good new therapeutic L-asparaginase?
Beckett et al. (2019)
3 more

3 mentions without citation

The differential ability of asparagine and glutamine in promoting the closed/active enzyme conformation rationalizes the Wolinella succinogenes L-asparaginase substrate specificity.
Nguyen et al. (2017)
2 more