6qgs

X-ray diffraction
2.76Å resolution

Crystal structure of APT1 bound to palmitic acid.

Released:

Function and Biology Details

Reaction catalysed:
Palmitoyl-[protein] + H(2)O = palmitate + [protein]
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-131082 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-protein thioesterase 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 233 amino acids
Theoretical weight: 24.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75608 (Residues: 1-230; Coverage: 100%)
Gene names: APT1, LPL1, LYPLA1
Sequence domains: Phospholipase/Carboxylesterase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P41212
Unit cell:
a: 81.66Å b: 81.66Å c: 441.946Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.23
Expression system: Escherichia coli