PDBe 3ika

X-ray diffraction
2.9Å resolution

Crystal Structure of EGFR 696-1022 T790M Mutant Covalently Binding to WZ4002


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

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Epidermal growth factor receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 331 amino acids
Theoretical weight: 37.66 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
  • Canonical: P00533 (Residues: 694-1022; Coverage: 28%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 48.23Å b: 89.126Å c: 165.224Å
α: 90° β: 90° γ: 90°
R R work R free
0.21 0.208 0.257
Expression system: Spodoptera frugiperda