› 2jit

X-ray diffraction
3.1Å resolution

Crystal structure of EGFR kinase domain T790M mutation

Released:
DOI: 10.2210/pdb2jit/pdb
PDB entry 2jit coloured by chain, front view.
PDB entry 2jit coloured by chain, side view.
PDB entry 2jit coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP.
Yun CH, Mengwasser KE, Toms AV, Woo MS, Greulich H, Wong KK, Meyerson M, Eck MJ
Proc Natl Acad Sci U S A 105 2070-5 (2008)
PMID: 18227510

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 327 amino acids
Theoretical weight: 37.33 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
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 53.889Å b: 90.304Å c: 164.347Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.249
Expression system: Spodoptera frugiperda

Quick links

Citations

405 review citations

Liquid biopsy: monitoring cancer-genetics in the blood.
Crowley et al. (2013)
404 more

21 mentions without citation

Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.
Muller et al. (2019)
20 more