› 5hw0

X-ray diffraction
1.7Å resolution

Erwinia chrysanthemi L-asparaginase + Glutamic acid

Released:
DOI: 10.2210/pdb5hw0/pdb
PDB entry 5hw0 coloured by chain, front view.
PDB entry 5hw0 coloured by chain, side view.
PDB entry 5hw0 coloured by chain, top view.
Source organism: Dickeya chrysanthemi
Primary publication:
Structural Insight into Substrate Selectivity of Erwinia chrysanthemi L-asparaginase.
Nguyen HA, Su Y, Lavie A
OpenAccess logo Biochemistry 55 1246-53 (2016)
PMID: 26855287

Function and Biology Details

Reaction catalysed: 
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

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: 328 amino acids
Theoretical weight: 35.29 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
  • Canonical: P06608 (Residues: 23-348; Coverage: 100%)
Gene names: ansB, asn
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 75.24Å b: 88.818Å c: 174.573Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.205
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Development of L-Asparaginase Biobetters: Current Research Status and Review of the Desirable Quality Profiles.
Brumano et al. (2018)
3 more

2 mentions without citation

Design and Characterization of Erwinia Chrysanthemi l-Asparaginase Variants with Diminished l-Glutaminase Activity.
Nguyen et al. (2016)
1 more