PDBe 1apy

X-ray diffraction
2Å resolution

HUMAN ASPARTYLGLUCOSAMINIDASE

Released:
Source organism: Homo sapiens
Primary publication:
Three-dimensional structure of human lysosomal aspartylglucosaminidase.
Nat. Struct. Biol. 2 1102-8 (1995)
PMID: 8846222

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)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glycosylasparaginase alpha chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 162 amino acids
Theoretical weight: 17.29 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P20933 (Residues: 24-185; Coverage: 50%)
Gene name: AGA
Glycosylasparaginase beta chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 141 amino acids
Theoretical weight: 15.09 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P20933 (Residues: 206-346; Coverage: 44%)
Gene name: AGA
Structure domains: (Glycosyl)asparaginase

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P61
Unit cell:
a: 98.4Å b: 98.4Å c: 134.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.169 0.224