5jge

X-ray diffraction
1.91Å resolution

Crystal structure of Atg19 coiled-coil complexed with Ape1 propeptide

Released:

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:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Autophagy-related protein 19 Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 32 amino acids
Theoretical weight: 3.8 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P35193 (Residues: 160-187; Coverage: 7%)
Gene names: ATG19, CVT19, O0980, YOL01, YOL082W
Vacuolar aminopeptidase 1 Chains: C, F
Molecule details ›
Chains: C, F
Length: 23 amino acids
Theoretical weight: 2.78 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P14904 (Residues: 1-20; Coverage: 4%)
Gene names: APE1, API, LAP4, YKL103C, YKL455, YSC1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P1
Unit cell:
a: 27.875Å b: 32.921Å c: 56.957Å
α: 87.19° β: 76.52° γ: 67.1°
R-values:
R R work R free
0.197 0.194 0.246
Expression system: Escherichia coli