› 4r8l

X-ray diffraction
2.41Å resolution

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

Released:
DOI: 10.2210/pdb4r8l/pdb
PDB entry 4r8l coloured by chain, front view.
PDB entry 4r8l coloured by chain, side view.
PDB entry 4r8l coloured by chain, top view.
Source organism: Cavia porcellus
Primary publication:
Identification and structural analysis of an L-asparaginase enzyme from guinea pig with putative tumor cell killing properties.
Schalk AM, Nguyen HA, Rigouin C, Lavie A
J Biol Chem 289 33175-86 (2014)
PMID: 25320094

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124711 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • Canonical: H0W0T5 (Residues: 1-362; Coverage: 64%)
Gene name: ASPG
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-G
Spacegroup: I222
Unit cell:
a: 123.21Å b: 156Å c: 158.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.206 0.236
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Novel Insights on the Use of L-Asparaginase as an Efficient and Safe Anti-Cancer Therapy.
Van Trimpont et al. (2022)
3 more

5 mentions without citation

Identification and structural analysis of an L-asparaginase enzyme from guinea pig with putative tumor cell killing properties.
Schalk et al. (2014)
4 more