› 5sv7

X-ray diffraction
3.21Å resolution

The Crystal structure of a chaperone

Released:
DOI: 10.2210/pdb5sv7/pdb
PDB entry 5sv7 coloured by chain, front view.
PDB entry 5sv7 coloured by chain, side view.
PDB entry 5sv7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins.
Wang P, Li J, Sha B
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
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192756 (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)

Quick links

Citations

10 review citations

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum.
Karagöz et al. (2019)
9 more

2 mentions without citation

The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization.
Wang et al. (2018)
1 more