› 2ito

X-ray diffraction
3.25Å resolution

Crystal structure of EGFR kinase domain G719S mutation in complex with Iressa

Released:
DOI: 10.2210/pdb2ito/pdb
PDB entry 2ito coloured by chain, front view.
PDB entry 2ito coloured by chain, side view.
PDB entry 2ito coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity.
Yun CH, Boggon TJ, Li Y, Woo MS, Greulich H, Meyerson M, Eck MJ
Cancer Cell 11 217-27 (2007)
PMID: 17349580

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epidermal growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 327 amino acids
Theoretical weight: 37.33 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 696-1022; Coverage: 28%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand IRE 1 x IRE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I23
Unit cell:
a: 142.929Å b: 142.929Å c: 142.929Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.189 0.266
Expression system: Spodoptera frugiperda

Quick links

Citations

142 review citations

EGFR antagonists in cancer treatment.
Ciardiello et al. (2008)
141 more

28 mentions without citation

Structure and clinical relevance of the epidermal growth factor receptor in human cancer.
Kumar et al. (2008)
27 more