1p4k

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT

Released:
Primary publication:
A dual role for an aspartic acid in glycosylasparaginase autoproteolysis.
Structure 11 997-1003 (2003)
PMID: 12906830

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase Chains: A, C
Molecule details ›
Chains: A, C
Length: 295 amino acids
Theoretical weight: 32.18 KDa
Source organism: Elizabethkingia meningoseptica
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47898 (Residues: 46-340; Coverage: 100%)
Sequence domains: Asparaginase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P1
Unit cell:
a: 46.176Å b: 52.717Å c: 61.924Å
α: 80.85° β: 90.21° γ: 105.08°
R-values:
R R work R free
0.182 0.182 0.22
Expression system: Escherichia coli