› 5i48

X-ray diffraction
1.5Å resolution

Erwinia chrysanthemi L-asparaginase A31I + E63Q mutation + Aspartic acid

Released:
DOI: 10.2210/pdb5i48/pdb
PDB entry 5i48 coloured by chain, front view.
PDB entry 5i48 coloured by chain, side view.
PDB entry 5i48 coloured by chain, top view.
Source organism: Dickeya chrysanthemi
Primary publication:
Design and Characterization of Erwinia Chrysanthemi l-Asparaginase Variants with Diminished l-Glutaminase Activity.
Nguyen HA, Su Y, Lavie A
J Biol Chem 291 17664-76 (2016)
PMID: 27354283

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-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: 35.33 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 ASP 4 x ASP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 77.188Å b: 87.691Å c: 175.108Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.123 0.12 0.171
Expression system: Escherichia coli

Quick links

Citations

8 review citations

What makes a good new therapeutic L-asparaginase?
Beckett et al. (2019)
7 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