2gu2

X-ray diffraction
1.8Å resolution

Crystal Structure of an Aspartoacylase from Rattus norvegicus

Released:
Source organism: Rattus norvegicus
Primary publication:
Structure of aspartoacylase, the brain enzyme impaired in Canavan disease.
Proc Natl Acad Sci U S A 104 456-61 (2007)
PMID: 17194761

Function and Biology Details

Reaction catalysed:
N-acyl-L-aspartate + H(2)O = a carboxylate + L-aspartate
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-193096 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartoacylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 312 amino acids
Theoretical weight: 35.47 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9R1T5 (Residues: 2-312; Coverage: 100%)
Gene name: Aspa
Sequence domains: Succinylglutamate desuccinylase / Aspartoacylase family
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 92.581Å b: 135.778Å c: 54.033Å
α: 90° β: 101.49° γ: 90°
R-values:
R R work R free
0.152 0.149 0.194
Expression system: Escherichia coli