PDBe 5xdl

X-ray diffraction
2.7Å resolution

Crystal structure of EGFR 696-1022 L858R in complex with CO-1686

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of mutant-selectivity and drug-resistance related to CO-1686.
OpenAccess logo Oncotarget 8 53508-53517 (2017)
PMID: 28881827

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:
Epidermal growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 37.68 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: NEW P00533 (Residues: 696-1022; Coverage: 28%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine kinase

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I23
Unit cell:
a: 143.543Å b: 143.543Å c: 143.543Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.256
Expression system: Spodoptera frugiperda