› 1fj2

X-ray diffraction
1.5Å resolution

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

Released:
DOI: 10.2210/pdb1fj2/pdb
PDB entry 1fj2 coloured by chain, front view.
PDB entry 1fj2 coloured by chain, side view.
PDB entry 1fj2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A.
Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS
Structure 8 1137-46 (2000)
PMID: 11080636

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-131082 (preferred)
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: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand BR 40 x BR
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

Quick links

Citations

18 review citations

The metabolic serine hydrolases and their functions in mammalian physiology and disease.
Long et al. (2011)
17 more

24 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
23 more