X-ray diffraction
1.4Å resolution

Crystal structure of the unphosphorylated IRAK4 kinase domain Bound to a type I inhibitor


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Interleukin-1 receptor-associated kinase 4 Chains: A, D
Molecule details ›
Chains: A, D
Length: 302 amino acids
Theoretical weight: 33.72 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
  • Canonical: Q9NWZ3 (Residues: 164-460; Coverage: 65%)
Gene name: IRAK4
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 70.888Å b: 58.553Å c: 76.101Å
α: 90° β: 112.78° γ: 90°
R R work R free
0.179 0.178 0.201
Expression system: Trichoplusia ni