› 2p2n

X-ray diffraction
1.9Å resolution

Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I

Released:
DOI: 10.2210/pdb2p2n/pdb
PDB entry 2p2n coloured by chain, front view.
PDB entry 2p2n coloured by chain, side view.
PDB entry 2p2n coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I.
Yun MK, Nourse A, White SW, Rock CO, Heath RJ
J Mol Biol 369 794-811 (2007)
PMID: 17451745

Function and Biology Details

Reaction catalysed: 
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-asparaginase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 358 amino acids
Theoretical weight: 39.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A962 (Residues: 1-338; Coverage: 100%)
Gene names: JW1756, ansA, b1767
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CL 4 x CL
Ligand ASP 4 x ASP
Ligand ASN 8 x ASN
Ligand EDO 12 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 90.315Å b: 89.757Å c: 93.083Å
α: 90° β: 117.03° γ: 90°
R-values:
R R work R free
0.223 0.223 0.264
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Dynamic dissociating homo-oligomers and the control of protein function.
Selwood et al. (2012)
4 more

4 mentions without citation

Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity.
Loch et al. (2021)
3 more