PDBe 4wd5

X-ray diffraction
3.3Å resolution

Crystal structure of EGFR 696-1022 T790M in complex with QL-X138

Released:
Source organism: Homo sapiens
Entry authors: Yun CH, Eck MJ

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

Assemblies composition:
monomeric
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: P00533 (Residues: 694-1022; Coverage: 28%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 47.575Å b: 93.288Å c: 163.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.21 0.239
Expression system: Spodoptera frugiperda