X-ray diffraction
2.1Å resolution

Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria


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
N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 32.24 KDa
Source organism: Elizabethkingia miricola
Expression system: Escherichia coli
  • 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 X29A
Spacegroup: P1
Unit cell:
a: 45.81Å b: 50.62Å c: 61.23Å
α: 86.28° β: 91.04° γ: 107.75°
R R work R free
0.194 0.19 0.252
Expression system: Escherichia coli