› 5ugc

X-ray diffraction
1.58Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epidermal growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 37.58 KDa
Source organism: Homo sapiens
Expression system: Spodoptera aff. frugiperda 2 RZ-2014
UniProt:
  • Canonical: P00533 (Residues: 695-1022; Coverage: 28%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand 8BS 1 x 8BS
Ligand SO4 2 x SO4
Ligand GOL 3 x GOL
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 34.722Å b: 69.62Å c: 112.029Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.223
Expression system: Spodoptera aff. frugiperda 2 RZ-2014

Quick links

Citations

10 review citations

Management of acquired resistance to EGFR TKI-targeted therapy in advanced non-small cell lung cancer.
Wu et al. (2018)
9 more

11 mentions without citation

Proteome-wide Map of Targets of T790M-EGFR-Directed Covalent Inhibitors.
Niessen et al. (2017)
10 more