6jxt

X-ray diffraction
2.31Å resolution

Crystal structure of EGFR 696-1022 WT in complex with AZD9291 prepared by cocrystallization

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
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: 37.45 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

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P3221
Unit cell:
a: 86.749Å b: 86.749Å c: 103.939Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.216 0.239
Expression system: Spodoptera frugiperda