› 1agx

X-ray diffraction
2.9Å resolution

REFINED CRYSTAL STRUCTURE OF ACINETOBACTER GLUTAMINASIFICANS GLUTAMINASE-ASPARAGINASE

Released:
DOI: 10.2210/pdb1agx/pdb
PDB entry 1agx coloured by chain, front view.
PDB entry 1agx coloured by chain, side view.
PDB entry 1agx coloured by chain, top view.
Source organism: Acinetobacter glutaminasificans
Primary publication:
Refined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.
Lubkowski J, Wlodawer A, Housset D, Weber IT, Ammon HL, Murphy KC, Swain AL
Acta Crystallogr D Biol Crystallogr 50 826-32 (1994)
PMID: 15299349

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-145196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminase-asparaginase Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 35.52 KDa
Source organism: Acinetobacter glutaminasificans
Expression system: Not provided
UniProt:
  • Canonical: P10172 (Residues: 1-331; Coverage: 100%)
Gene name: ansB
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 96.6Å b: 112.5Å c: 71.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 not available
Expression system: Not provided

Quick links

Citations

4 review citations

Where freedom is given, liberties are taken.
Kleywegt et al. (1995)
3 more

2 mentions without citation

The differential ability of asparagine and glutamine in promoting the closed/active enzyme conformation rationalizes the Wolinella succinogenes L-asparaginase substrate specificity.
Nguyen et al. (2017)
1 more