› 2a91

X-ray diffraction
2.5Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138062 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Receptor tyrosine-protein kinase erbB-2 Chain: A
Molecule details ›
Chain: A
Length: 517 amino acids
Theoretical weight: 56.99 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P04626 (Residues: 22-530; Coverage: 41%)
Gene names: ERBB2, HER2, MLN19, NEU, NGL
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 75.957Å b: 82.243Å c: 110.063Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.226 0.264
Expression system: Cricetulus griseus

Quick links

Citations

127 review citations

ERBB receptors and cancer: the complexity of targeted inhibitors.
Hynes et al. (2005)
126 more

17 mentions without citation

Protein Kinase Targets in Breast Cancer.
García-Aranda et al. (2017)
16 more