PDBe 4rix

X-ray diffraction
3.1Å resolution

Crystal structure of an EGFR/HER3 kinase domain heterodimer containing the cancer-associated HER3-Q790R mutation

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Receptor tyrosine-protein kinase erbB-3 Chains: A, C
Molecule details ›
Chains: A, C
Length: 326 amino acids
Theoretical weight: 36.52 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P21860 (Residues: 698-1020; Coverage: 24%)
Gene names: ERBB3, HER3
Sequence domains: Protein tyrosine kinase
Structure domains:
Epidermal growth factor receptor Chains: B, D
Molecule details ›
Chains: B, D
Length: 345 amino acids
Theoretical weight: 39.17 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 682-1022; Coverage: 29%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 64.649Å b: 155.053Å c: 86.857Å
α: 90° β: 111.09° γ: 90°
R-values:
R R work R free
0.21 0.207 0.258
Expression system: Spodoptera frugiperda