› 1hg0

X-ray diffraction
1.9Å resolution

X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and succinic acid

Released:
DOI: 10.2210/pdb1hg0/pdb
PDB entry 1hg0 coloured by chain, front view.
PDB entry 1hg0 coloured by chain, side view.
PDB entry 1hg0 coloured by chain, top view.
Source organism: Dickeya chrysanthemi
Primary publication:
Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase.
Aghaiypour K, Wlodawer A, Lubkowski J
Biochemistry 40 5655-64 (2001)
PMID: 11341830

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139091 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-asparaginase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 327 amino acids
Theoretical weight: 35.12 KDa
Source organism: Dickeya chrysanthemi
UniProt:
  • Canonical: P06608 (Residues: 22-348; Coverage: 100%)
Gene names: ansB, asn
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SIN 4 x SIN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 107.18Å b: 91.32Å c: 128.41Å
α: 90° β: 92.04° γ: 90°
R-values:
R R work R free
0.171 0.171 0.199

Quick links

Citations

13 review citations

From one amino acid to another: tRNA-dependent amino acid biosynthesis.
Sheppard et al. (2008)
12 more

2 mentions without citation

Identification and structural analysis of an L-asparaginase enzyme from guinea pig with putative tumor cell killing properties.
Schalk et al. (2014)
1 more