› 6paa

X-ray diffraction
1.85Å resolution

E. coli L-asparaginase II mutant (T12V) in complex with L-Asp at pH 5.5

Released:
DOI: 10.2210/pdb6paa/pdb
PDB entry 6paa coloured by chain, front view.
PDB entry 6paa coloured by chain, side view.
PDB entry 6paa 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: 35.7 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 151.837Å b: 62.472Å c: 143.373Å
α: 90° β: 118.11° γ: 90°
R-values:
R R work R free
0.173 0.17 0.229
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

1 mention without citation

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