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:
Vacuolar aminopeptidase 1 (preferred)
PDBe Complex ID:
PDB-CPX-147137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar aminopeptidase 1
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)
UniProt:
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:
Length: 470 amino acids
Theoretical weight: 51.89 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P14904 (Residues: 46-514; Coverage: 91%)
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
NSRRC BEAMLINE BL15A
Spacegroup:
R3
Expression system: Escherichia coli BL21(DE3)
