› 2p2d

X-ray diffraction
1.89Å resolution

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

Released:
DOI: 10.2210/pdb2p2d/pdb
PDB entry 2p2d coloured by chain, front view.
PDB entry 2p2d coloured by chain, side view.
PDB entry 2p2d 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

1 bound ligand:
Ligand GOL 12 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 57.763Å b: 151.586Å c: 87.142Å
α: 90° β: 88.63° γ: 90°
R-values:
R R work R free
0.184 0.184 0.207
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

5 mentions without citation

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