› 5jh9

X-ray diffraction
2.1Å 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: 516 amino acids
Theoretical weight: 57.29 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P14904 (Residues: 1-514; Coverage: 100%)
Gene names: APE1, API, LAP4, YKL103C, YKL455, YSC1
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 8 x ZN
Ligand CAC 8 x CAC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: R3
Unit cell:
a: 140.428Å b: 140.428Å c: 348.922Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.207
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