PDBe 3eca

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF ESCHERICHIA COLI L-ASPARAGINASE, AN ENZYME USED IN CANCER THERAPY

Released:
Source organism: Escherichia coli

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-asparaginase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 326 amino acids
Theoretical weight: 34.63 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P00805 (Residues: 23-348; Coverage: 100%)
Gene names: JW2924, ansB, b2957
Sequence domains: Asparaginase, N-terminal
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 76.7Å b: 96.1Å c: 111.3Å
α: 90° β: 97.1° γ: 90°
R-values:
R R work R free
0.149 0.149 not available
Expression system: Not provided