PDBe 3kex

X-ray diffraction
2.8Å resolution

Crystal structure of the catalytically inactive kinase domain of the human epidermal growth factor receptor 3 (HER3)

Released:
Source organism: Homo sapiens
Primary publication:
Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3.
Proc. Natl. Acad. Sci. U.S.A. 106 21608-13 (2009)
PMID: 20007378

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor tyrosine-protein kinase erbB-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 325 amino acids
Theoretical weight: 36.45 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P21860 (Residues: 698-1019; Coverage: 24%)
Gene names: ERBB3, HER3
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2
Unit cell:
a: 194.164Å b: 47.637Å c: 81.281Å
α: 90° β: 108.04° γ: 90°
R-values:
R R work R free
0.243 0.241 0.283
Expression system: Spodoptera frugiperda