› 1ho3

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE ANALYSIS OF E. COLI L-ASPARAGINASE II (Y25F MUTANT)

Released:
DOI: 10.2210/pdb1ho3/pdb
PDB entry 1ho3 coloured by chain, front view.
PDB entry 1ho3 coloured by chain, side view.
PDB entry 1ho3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.
Jaskólski M, Kozak M, Lubkowski J, Palm G, Wlodawer A
Acta Crystallogr D Biol Crystallogr 57 369-77 (2001)
PMID: 11223513

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-133590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-asparaginase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 34.61 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00805 (Residues: 23-348; Coverage: 100%)
Gene names: JW2924, ansB, b2957
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ASP 2 x ASP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P6522
Unit cell:
a: 80.999Å b: 80.999Å c: 341.075Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.182 0.245
Expression system: Escherichia coli

Quick links

Citations

5 review citations

A Comprehensive Review on L-Asparaginase and Its Applications.
Batool et al. (2016)
4 more

2 mentions without citation

Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
Lubkowski et al. (2019)
1 more