PDBe 5zwj

X-ray diffraction
2.9Å resolution

Crystal structure of EGFR 675-1022 T790M/C797S/V948R in complex with EAI045

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of EGFR T790M/C797S/V948R in complex with EAI045.
Biochem. Biophys. Res. Commun. 502 332-337 (2018)
PMID: 29802850

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: 355 amino acids
Theoretical weight: 40.84 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 675-1022; Coverage: 29%)
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: P6122
Unit cell:
a: 79.586Å b: 79.586Å c: 215.075Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.256 0.255 0.272
Expression system: Spodoptera frugiperda