Crystal structure of EGFR-T790M/V948R in complex with osimertinib and EAI045

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).

Ligands and binding sites

• Q6K · ~{N}-[2-[2-(dimethylamino)ethyl-methyl-amino]-4-methoxy-5-[[4-(1-methylindol-3-yl)pyrimidin-2-yl]amino]phenyl]propanamide · ligand · 2 copies · chains A, B
• 9LL · (2R)-2-(5-fluoro-2-hydroxyphenyl)-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)-N-(1,3-thiazol-2-yl)acetamide · ligand · 2 copies · chains A, B
• SO4 · Sulfate ion · ion · 10 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1198 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 6Z4B · Crystal Structure of EGFR-T790M/V948R in Complex with Osimertinib and EAI045 · the same entry in another collection · chain A against A, TM-score 1.00
• P00533 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor (P00533) · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P00533
• Elsewhere: RCSB PDB 6Z4B · PDBe 6Z4B · UniProt P00533