X-ray diffraction
2.5Å resolution

Crystal structure of yeast aminopeptidase 1 (Ape1)


Function and Biology Details

Reaction catalysed:
Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-147137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Vacuolar aminopeptidase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 470 amino acids
Theoretical weight: 51.89 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P14904 (Residues: 46-514; Coverage: 91%)
Gene names: APE1, API, LAP4, YKL103C, YKL455, YSC1
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL15A
Spacegroup: R3
Unit cell:
a: 140.171Å b: 140.171Å c: 348.677Å
α: 90° β: 90° γ: 120°
R R work R free
0.217 0.215 0.246
Expression system: Escherichia coli BL21(DE3)