› 1u6d

X-ray diffraction
1.85Å resolution

Crystal structure of the Kelch domain of human Keap1

Released:
DOI: 10.2210/pdb1u6d/pdb
PDB entry 1u6d coloured by chain, front view.
PDB entry 1u6d coloured by chain, side view.
PDB entry 1u6d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the Kelch domain of human Keap1.
Li X, Zhang D, Hannink M, Beamer LJ
J Biol Chem 279 54750-8 (2004)
PMID: 15475350

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: X
Molecule details ›
Chain: X
Length: 308 amino acids
Theoretical weight: 33.69 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
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6522
Unit cell:
a: 85.892Å b: 85.892Å c: 148.753Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.149 0.148 0.182
Expression system: Escherichia coli

Quick links

Citations

48 review citations

Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway.
Kensler et al. (2007)
47 more

22 mentions without citation

In silico structure-based approaches to discover protein-protein interaction-targeting drugs.
Shin et al. (2017)
21 more