X-ray diffraction
2.55Å resolution

Acylaminoacyl peptidase complexed with a chloromethylketone inhibitor


Function and Biology Details

Reaction catalysed:
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Acylamino-acid-releasing enzyme Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 582 amino acids
Theoretical weight: 63.11 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
  • Canonical: Q9YBQ2 (Residues: 1-582; Coverage: 100%)
Gene name: APE_1547.1
Sequence domains: Prolyl oligopeptidase family
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 71.58Å b: 97.3Å c: 99.16Å
α: 105.15° β: 103.96° γ: 100.26°
R R work R free
0.214 0.212 0.26
Expression system: Escherichia coli