PDBe 3qd2

X-ray diffraction
2.81Å resolution

Crsytal structure of mouse PERK kinase domain

Source organism: Mus musculus
Primary publication:
The structure of the PERK kinase domain suggests the mechanism for its activation.
Acta Crystallogr. D Biol. Crystallogr. 67 423-8 (2011)
PMID: 21543844

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Eukaryotic translation initiation factor 2-alpha kinase 3 Chain: B
Molecule details ›
Chain: B
Length: 332 amino acids
Theoretical weight: 38.67 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
  • Canonical: Q9Z2B5 (Residues: 582-1078; Coverage: 31%)
Gene names: Eif2ak3, Pek, Perk
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P41212
Unit cell:
a: 97.891Å b: 97.891Å c: 116.706Å
α: 90° β: 90° γ: 90°
R R work R free
0.273 0.27 0.332
Expression system: Escherichia coli BL21