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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
Vacuolar aminopeptidase 1 (preferred)
PDBe Complex ID:
PDB-CPX-147138 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar aminopeptidase 1
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, j, k, l, m
Length: 24 amino acids
Theoretical weight: 2.86 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Length: 24 amino acids
Theoretical weight: 2.86 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
P14904 (Residues: 1-22; Coverage: 4%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup:
R32
Expression system: Escherichia coli
