Structural basis for the defects of human lung cancer somatic mutations in the repression activity of KEAP1 on NRF2

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 52% strand (DSSP).

Ligands and binding sites

• SO4 · Sulfate ion · ion · 9 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 574 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

• 1X2R · Structural basis for the defects of human lung cancer somatic mutations in the repression… · the same entry in another collection · chain A against A, TM-score 1.00
• Q9Z2X8 · AlphaFold monomer V2.0 prediction for kelch-like ech-associated protein 1 (Q9Z2X8) · a predicted model of the same protein · chain A against A, TM-score 1.00
• Q60795 · AlphaFold monomer V2.0 prediction for nuclear factor erythroid 2-related factor 2 (Q60795) · a predicted model of the same protein · chain B against A, TM-score 0.80

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 Q9Z2X8
• Every structure of UniProt Q60795
• Elsewhere: RCSB PDB 1X2R · PDBe 1X2R · UniProt Q9Z2X8 · UniProt Q60795