6egd

X-ray diffraction
2.1Å resolution

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

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: Q9NWZ3 (Residues: 164-460; Coverage: 65%)
Gene name: IRAK4
Sequence domains: Protein tyrosine kinase

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 71.45Å b: 59.5Å c: 75.62Å
α: 90° β: 111.81° γ: 90°
R-values:
R R work R free
0.184 0.181 0.23
Expression system: Trichoplusia ni