X-ray diffraction
2.41Å resolution

Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain


Function and Biology Details

Reaction catalysed:
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Asparaginase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 385 amino acids
Theoretical weight: 41.98 KDa
Source organism: Cavia porcellus
Expression system: Escherichia coli BL21(DE3)
  • Canonical: H0W0T5 (Residues: 1-362; Coverage: 64%)
Gene name: ASPG
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: I222
Unit cell:
a: 123.21Å b: 156Å c: 158.82Å
α: 90° β: 90° γ: 90°
R R work R free
0.207 0.206 0.236
Expression system: Escherichia coli BL21(DE3)