› 4l7b

X-ray diffraction
2.41Å resolution

Structure of keap1 kelch domain with (1S,2R)-2-{[(1S)-1-[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-3,4-dihydroisoquinolin-2(1H)-yl]carbonyl}cyclohexanecarboxylic acid

Released:
DOI: 10.2210/pdb4l7b/pdb
PDB entry 4l7b coloured by chain, front view.
PDB entry 4l7b coloured by chain, side view.
PDB entry 4l7b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding mode and structure-activity relationships around direct inhibitors of the Nrf2-Keap1 complex.
Jnoff E, Albrecht C, Barker JJ, Barker O, Beaumont E, Bromidge S, Brookfield F, Brooks M, Bubert C, Ceska T, Corden V, Dawson G, Duclos S, Fryatt T, Genicot C, Jigorel E, Kwong J, Maghames R, Mushi I, Pike R, Sands ZA, Smith MA, Stimson CC, Courade JP
ChemMedChem 9 699-705 (2014)
PMID: 24504667

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171937 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kelch-like ECH-associated protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 300 amino acids
Theoretical weight: 33.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14145 (Residues: 321-609; Coverage: 46%)
Gene names: INRF2, KEAP1, KIAA0132, KLHL19
Sequence domains: Kelch motif
Structure domains: Kelch-type beta propeller

Ligands and Environments

3 bound ligands:
Ligand ACT 5 x ACT
Ligand 1VV 1 x 1VV
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 75.76Å b: 75.85Å c: 205.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.246
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Activators and Inhibitors of NRF2: A Review of Their Potential for Clinical Development.
Robledinos-Antón et al. (2019)
11 more

40 mentions without citation

Structural basis of Keap1 interactions with Nrf2.
Canning et al. (2015)
39 more