6d3l

X-ray diffraction
3.1Å resolution

Crystal structure of unphosphorylated human PKR

Released:
Source organism: Homo sapiens
Primary publication:
Structural Basis of Protein Kinase R Autophosphorylation.
Biochemistry 58 2967-2977 (2019)
PMID: 31246429

Function and Biology Details

Reactions catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-148631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interferon-induced, double-stranded RNA-activated protein kinase Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 37.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19525 (Residues: 229-551; Coverage: 59%)
Gene names: EIF2AK2, PKR, PRKR
Sequence domains: Protein kinase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-2
Spacegroup: P6122
Unit cell:
a: 92.689Å b: 92.689Å c: 123.325Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.263 0.258 0.347
Expression system: Escherichia coli