› 4o47

X-ray diffraction
1.9Å resolution

Crystal structure of uncleaved guinea pig L-asparaginase type III

Released:
DOI: 10.2210/pdb4o47/pdb
PDB entry 4o47 coloured by chain, front view.
PDB entry 4o47 coloured by chain, side view.
PDB entry 4o47 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
OpenAccess logo 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-164933 (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

1 bound ligand:
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P3221
Unit cell:
a: 114.872Å b: 114.872Å c: 138.971Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.193 0.213
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

2 mentions without citation

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