PDBe 5xgm

X-ray diffraction
2.95Å resolution

Crystal structure of EGFR 696-1022 T790M in complex with Go6976

Released:
Source organism: Homo sapiens
Primary publication:
Structural pharmacological studies on EGFR T790M/C797S.
Biochem. Biophys. Res. Commun. 488 266-272 (2017)
PMID: 28456628

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: 37.65 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 kinase

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: I23
Unit cell:
a: 146.31Å b: 146.31Å c: 146.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.203 0.232
Expression system: Spodoptera frugiperda