› 1zgk

X-ray diffraction
1.35Å resolution

1.35 angstrom structure of the Kelch domain of Keap1

Released:
DOI: 10.2210/pdb1zgk/pdb
PDB entry 1zgk coloured by chain, front view.
PDB entry 1zgk coloured by chain, side view.
PDB entry 1zgk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1.
Beamer LJ, Li X, Bottoms CA, Hannink M
Acta Crystallogr D Biol Crystallogr 61 1335-42 (2005)
PMID: 16204884

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171933 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kelch-like ECH-associated protein 1 Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 34.02 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

No bound ligands
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6522
Unit cell:
a: 85.745Å b: 85.745Å c: 147.818Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.112 0.111 0.133
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Small molecule modulators of Keap1-Nrf2-ARE pathway as potential preventive and therapeutic agents.
Magesh et al. (2012)
6 more

19 mentions without citation

Discovery of direct inhibitors of Keap1-Nrf2 protein-protein interaction as potential therapeutic and preventive agents.
Abed et al. (2015)
18 more