5jm9

Electron Microscopy
24Å 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:
Cellular component:

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar aminopeptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 514 amino acids
Theoretical weight: 57.16 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P14904 (Residues: 1-514; Coverage: 100%)
Gene names: APE1, API, LAP4, YKL103C, YKL455, YSC1
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 24Å
Relevant EMDB volumes: EMD-8167
Expression system: Escherichia coli BL21