› 1pja

X-ray diffraction
2.7Å resolution

The crystal structure of palmitoyl protein thioesterase-2 reveals the basis for divergent substrate specificities of the two lysosomal thioesterases (PPT1 and PPT2)

Released:
DOI: 10.2210/pdb1pja/pdb
PDB entry 1pja coloured by chain, front view.
PDB entry 1pja coloured by chain, side view.
PDB entry 1pja coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2.
Calero G, Gupta P, Nonato MC, Tandel S, Biehl ER, Hofmann SL, Clardy J
J Biol Chem 278 37957-64 (2003)
PMID: 12855696

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193969 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysosomal thioesterase PPT2 Chain: A
Molecule details ›
Chain: A
Length: 302 amino acids
Theoretical weight: 34.34 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9UMR5 (Residues: 1-302; Coverage: 100%)
Gene name: PPT2
Sequence domains: Palmitoyl protein thioesterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand NAG 1 x NAG
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P6222
Unit cell:
a: 148.52Å b: 148.52Å c: 152.51Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.251 0.221 0.242
Expression system: Spodoptera frugiperda

Quick links

Citations

11 review citations

Putting proteins in their place: palmitoylation in Huntington disease and other neuropsychiatric diseases.
Young et al. (2012)
10 more

9 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
8 more