PDBe 3zgd

X-ray diffraction
1.98Å resolution

crystal structure of a KEAP1 mutant

Released:
Source organism: Homo sapiens
Primary publication:
Crystal-contact engineering to obtain a crystal form of the Kelch domain of human Keap1 suitable for ligand-soaking experiments.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 592-6 (2013)
PMID: 23722832

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kelch-like ECH-associated protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 310 amino acids
Theoretical weight: 33.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 75.72Å b: 75.77Å c: 202.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.181
Expression system: Escherichia coli BL21(DE3)