› 6pa3

X-ray diffraction
1.65Å resolution

E. coli L-asparaginase II double mutant (T89V,K162T) in complex with L-Asn at pH 7.0

Released:
DOI: 10.2210/pdb6pa3/pdb
PDB entry 6pa3 coloured by chain, front view.
PDB entry 6pa3 coloured by chain, side view.
PDB entry 6pa3 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
Lubkowski J, Wlodawer A
Protein Sci 28 1850-1864 (2019)
PMID: 31423681

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-133590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-asparaginase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 334 amino acids
Theoretical weight: 35.67 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00805 (Residues: 23-348; Coverage: 100%)
Gene names: JW2924, ansB, b2957
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand ASN 4 x ASN
Ligand IMD 3 x IMD
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 152.852Å b: 62.99Å c: 141.293Å
α: 90° β: 117.83° γ: 90°
R-values:
R R work R free
0.15 0.149 0.184
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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

4 mentions without citation

Characterization of a Novel L-Asparaginase from Mycobacterium gordonae with Acrylamide Mitigation Potential.
Chi et al. (2021)
3 more