› 6ege

X-ray diffraction
1.4Å resolution

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

Released:
DOI: 10.2210/pdb6ege/pdb
PDB entry 6ege coloured by chain, front view.
PDB entry 6ege coloured by chain, side view.
PDB entry 6ege coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4).
Wang L, Ferrao R, Li Q, Hatcher JM, Choi HG, Buhrlage SJ, Gray NS, Wu H
J Biol Chem 294 4511-4519 (2019)
PMID: 30679311

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192670 (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 and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand DL1 2 x DL1
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-values:
R R work R free
0.179 0.178 0.201
Expression system: Trichoplusia ni

Quick links

Citations

1 review citation

Tolerogenic dendritic cells and TLR4/IRAK4/NF-κB signaling pathway in allergic rhinitis.
Kang et al. (2023)
8 other articles

1 mention without citation

Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4).
Wang et al. (2019)