2gl9

X-ray diffraction
2Å resolution

Crystal Structure of Glycosylasparaginase-Substrate Complex

Released:
Primary publication:
Crystallographic snapshot of a productive glycosylasparaginase-substrate complex.
J Mol Biol 366 82-92 (2007)
PMID: 17157318

Function and Biology Details

Reaction catalysed:
N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-D-glucosaminylamine + L-aspartate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-175278 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glycosylasparaginase alpha chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 151 amino acids
Theoretical weight: 16.82 KDa
Source organism: Elizabethkingia meningoseptica
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47898 (Residues: 46-196; Coverage: 51%)
Sequence domains: Asparaginase
Glycosylasparaginase beta chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 144 amino acids
Theoretical weight: 15.38 KDa
Source organism: Elizabethkingia meningoseptica
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47898 (Residues: 197-340; Coverage: 49%)
Sequence domains: Asparaginase
Structure domains: (Glycosyl)asparaginase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 46.118Å b: 96.745Å c: 61.998Å
α: 90° β: 90.58° γ: 90°
R-values:
R R work R free
0.174 0.17 0.215
Expression system: Escherichia coli