6egf

X-ray diffraction
2.61Å resolution

Crystal structure of the inactive unphosphorylated IRAK4 kinase domain bound to AMP-PNP

Released:

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
Macromolecule:
Interleukin-1 receptor-associated kinase 4 Chain: B
Molecule details ›
Chain: B
Length: 302 amino acids
Theoretical weight: 33.72 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q9NWZ3 (Residues: 164-460; Coverage: 65%)
Gene name: IRAK4
Sequence domains: Protein tyrosine kinase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P6322
Unit cell:
a: 135.195Å b: 135.195Å c: 126.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.205 0.229
Expression system: Trichoplusia ni