› 2o53

X-ray diffraction
2.7Å resolution

Crystal structure of apo-Aspartoacylase from human brain

Released:
DOI: 10.2210/pdb2o53/pdb
PDB entry 2o53 coloured by chain, front view.
PDB entry 2o53 coloured by chain, side view.
PDB entry 2o53 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue.
Le Coq J, Pavlovsky A, Malik R, Sanishvili R, Xu C, Viola RE
Biochemistry 47 3484-92 (2008)
PMID: 18293939

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartoacylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 313 amino acids
Theoretical weight: 35.78 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P45381 (Residues: 1-313; Coverage: 100%)
Gene names: ACY2, ASP, ASPA
Sequence domains: Succinylglutamate desuccinylase / Aspartoacylase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P42212
Unit cell:
a: 143.794Å b: 143.794Å c: 104.076Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.216 0.269
Expression system: Komagataella pastoris

Quick links

Citations

1 review citation

A thematic review of scientific and family interests in Canavan Disease: where are the developmentalists?
Glicksman et al. (2013)
15 other articles

2 mentions without citation

Structures of aminoacylase 3 in complex with acetylated substrates.
Hsieh et al. (2010)
1 more