PDBe 4zse

X-ray diffraction
1.97Å resolution

Crystal structure of EGFR 696-1022 T790M/V948R, crystal form II

Released:
Source organism: Homo sapiens
Entry authors: Yan XE, Yun CH

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epidermal growth factor receptor Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 331 amino acids
Theoretical weight: 37.72 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: NEW P00533 (Residues: 695-1022; Coverage: 28%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 71.82Å b: 102.317Å c: 86.752Å
α: 90° β: 101.24° γ: 90°
R-values:
R R work R free
0.191 0.19 0.213
Expression system: Spodoptera frugiperda