1qu6

Solution NMR

STRUCTURE OF THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF THE PROTEIN KINASE PKR REVEALS THE MOLECULAR BASIS OF ITS DSRNA-MEDIATED ACTIVATION

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interferon-induced, double-stranded RNA-activated protein kinase Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 19.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19525 (Residues: 1-170; Coverage: 31%)
Gene names: EIF2AK2, PKR, PRKR
Sequence domains: Double-stranded RNA binding motif
Structure domains: Double Stranded RNA Binding Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: MODIFIED DG/SA PROTOCOL IN XPLOR
Expression system: Escherichia coli BL21(DE3)