› 4tnu

X-ray diffraction
2.9Å resolution

Human brain aspartoacylase mutant Y231C complex with intermediate analog (N-phosphonomethyl-L-aspartate)

Released:
DOI: 10.2210/pdb4tnu/pdb
PDB entry 4tnu coloured by chain, front view.
PDB entry 4tnu coloured by chain, side view.
PDB entry 4tnu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Aspartoacylase catalytic deficiency as the cause of Canavan disease: a structural perspective.
Wijayasinghe YS, Pavlovsky AG, Viola RE
Biochemistry 53 4970-8 (2014)
PMID: 25003821

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: 35.72 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 AS9 2 x AS9
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P42212
Unit cell:
a: 147.959Å b: 147.959Å c: 103.456Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.235
Expression system: Komagataella pastoris

Quick links

Citations

10 citation in other articles

Comparative computational assessment of the pathogenicity of mutations in the Aspartoacylase enzyme.
George Priya Doss et al. (2017)
9 more