PDBe 5sv7

X-ray diffraction
3.21Å resolution

The Crystal structure of a chaperone

Released:
Source organism: Homo sapiens
Primary publication:
The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins.
Acta Crystallogr D Struct Biol 72 1290-1297 (2016)
PMID: 27917829

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Eukaryotic translation initiation factor 2-alpha kinase 3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 326 amino acids
Theoretical weight: 36.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NZJ5 (Residues: 95-420; Coverage: 30%)
Gene names: EIF2AK3, PEK, PERK

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P32
Unit cell:
a: 163.913Å b: 163.913Å c: 63.076Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.273 0.27 0.322
Expression system: Escherichia coli BL21(DE3)