PDBe 1fj2

X-ray diffraction
1.5Å resolution

Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution

Released:

Function and Biology Details

Reaction catalysed:
1-alkyl-sn-glycero-3-phosphoethanolamine + H(2)O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-protein thioesterase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 232 amino acids
Theoretical weight: 24.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75608 (Residues: 6-230; Coverage: 98%)
Gene names: APT1, LPL1, LYPLA1
Sequence domains: Phospholipase/Carboxylesterase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21
Unit cell:
a: 39.59Å b: 127.89Å c: 39.66Å
α: 90° β: 102.8° γ: 90°
R-values:
R R work R free
0.183 0.183 0.237
Expression system: Escherichia coli