› 4o48

X-ray diffraction
2.29Å resolution

Crystal structure of cleaved guinea pig L-asparaginase type III in complex with L-aspartate

Released:
DOI: 10.2210/pdb4o48/pdb
PDB entry 4o48 coloured by chain, front view.
PDB entry 4o48 coloured by chain, side view.
PDB entry 4o48 coloured by chain, top view.
Source organism: Cavia porcellus
Primary publication:
Structural and kinetic characterization of guinea pig L-asparaginase type III.
Schalk AM, Lavie A
Biochemistry 53 2318-28 (2014)
PMID: 24669941

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 34.58 KDa
Source organism: Cavia porcellus
Expression system: Escherichia coli

Ligands and Environments

2 bound ligands:
Ligand NA 2 x NA
Ligand ASP 2 x ASP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P3221
Unit cell:
a: 114.58Å b: 114.58Å c: 138.59Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.221
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Therapeutic l-asparaginase: upstream, downstream and beyond.
Lopes et al. (2017)
6 more

1 mention without citation

Structural and kinetic characterization of guinea pig L-asparaginase type III.
Schalk et al. (2014)