› 2itq

X-ray diffraction
2.68Å resolution

Crystal structure of EGFR kinase domain G719S mutation in complex with AFN941

Released:
DOI: 10.2210/pdb2itq/pdb
PDB entry 2itq coloured by chain, front view.
PDB entry 2itq coloured by chain, side view.
PDB entry 2itq 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 ITQ 1 x ITQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: I23
Unit cell:
a: 145.291Å b: 145.291Å c: 145.291Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.263
Expression system: Spodoptera frugiperda

Quick links

Citations

143 review citations

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

6 mentions without citation

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