6qgq

X-ray diffraction
2.6Å resolution

Crystal structure of APT1 C2S mutant 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:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acyl-protein thioesterase 1 Chains: A, C, D
Molecule details ›
Chains: A, C, D
Length: 233 amino acids
Theoretical weight: 24.98 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
Acyl-protein thioesterase 1 Chain: B
Molecule details ›
Chain: B
Length: 234 amino acids
Theoretical weight: 25.05 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: P21212
Unit cell:
a: 146.138Å b: 160.738Å c: 40.679Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.238
Expression system: Escherichia coli