› 5jgf

X-ray diffraction
1.83Å resolution

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar aminopeptidase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 473 amino acids
Theoretical weight: 52.18 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • 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

1 bound ligand:
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: R3
Unit cell:
a: 140.969Å b: 140.969Å c: 348.917Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.162 0.179
Expression system: Escherichia coli

Quick links

Citations

5 review citations

History of the Selective Autophagy Research: How Did It Begin and Where Does It Stand Today?
Kirkin V. (2020)
4 more