› 3u0v

X-ray diffraction
1.72Å resolution

Function and Biology Details

Reaction catalysed: 
Palmitoyl-[protein] + H(2)O = palmitate + [protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysophospholipase-like protein 1 Chain: A
Molecule details ›
Chain: A
Length: 239 amino acids
Theoretical weight: 26.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5VWZ2 (Residues: 1-237; Coverage: 100%)
Gene name: LYPLAL1
Sequence domains: Phospholipase/Carboxylesterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 47.782Å b: 60.778Å c: 76.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.212
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Palmitoylation in Alzheimer's disease and other neurodegenerative diseases.
Cho et al. (2016)
10 more

7 mentions without citation

Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterases.
Bürger et al. (2012)
6 more