PDBe 6bfn

X-ray diffraction
2.26Å resolution

Crystal structure of human IRAK1

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human IRAK1.
Proc. Natl. Acad. Sci. U.S.A. (2017)
PMID: 29208712

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interleukin-1 receptor-associated kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 342 amino acids
Theoretical weight: 37.78 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P51617 (Residues: 194-530; Coverage: 47%)
Gene names: IRAK, IRAK1
Sequence domains: Protein kinase domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P41212
Unit cell:
a: 88.059Å b: 88.059Å c: 177.034Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.227
Expression system: Spodoptera frugiperda