PDBe 3zgc

X-ray diffraction
2.2Å resolution

crystal structure of the KEAP1-NEH2 complex

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

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
Nuclear factor erythroid 2-related factor 2 Chain: C
Molecule details ›
Chain: C
Length: 7 amino acids
Theoretical weight: 736 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q16236 (Residues: 76-82; Coverage: 1%)
Gene names: NFE2L2, NRF2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 76.103Å b: 76.064Å c: 207.541Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.188
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided