PDBe 3lmg

X-ray diffraction
2.8Å resolution

Crystal structure of the ERBB3 kinase domain in complex with AMP-PNP

Released:
Source organism: Homo sapiens
Primary publication:
ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation.
Proc. Natl. Acad. Sci. U.S.A. 107 7692-7 (2010)
PMID: 20351256

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor tyrosine-protein kinase erbB-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 38.73 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P21860 (Residues: 684-1020; Coverage: 26%)
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: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 193.348Å b: 47.981Å c: 82.224Å
α: 90° β: 108.11° γ: 90°
R-values:
R R work R free
0.255 0.252 0.285
Expression system: Spodoptera frugiperda