Acyl-protein thioesterase

Available protein structures:
PDB	IPR029058 PF02230 (ECOD; PDBsum)
AlphaFold	IPR029058; PF02230;

	Crystal structure of human APT1, PDB code 1fj2. Alpha helices are in red, beta strands in gold, catalytic site residues in black. The 2 different monomers of the dimer are shaded in green and brown.
Identifiers
Symbol	Acyl-protein thioesterases (APTs)
Pfam	PF02230
InterPro	IPR029058
PDB
Available protein structures:
PDB	IPR029058 PF02230 (ECOD; PDBsum)
AlphaFold	IPR029058; PF02230;

Acyl-protein thioesterases are enzymes that cleave off lipid modifications on proteins, located on the sulfur atom of cysteine residues linked via a thioester bond. Acyl-protein thioesterases are part of the α/β hydrolase superfamily of proteins and have a conserved catalytic triad. For that reason, acyl-protein thioesterases are also able to hydrolyze oxygen-linked ester bonds.