5sym

X-ray diffraction
1.55Å resolution

Cocrystal structure of the human acyl protein thioesterase 1 with an isoform-selective inhibitor, ML348

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-protein thioesterase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 230 amino acids
Theoretical weight: 24.69 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
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Unit cell:
a: 71.67Å b: 73.69Å c: 81.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.199
Expression system: Escherichia coli