› 4ifl

X-ray diffraction
1.8Å resolution

Crystal Structures of apo Keap1, Keap1-peptide, and Keap1-compound complexes

Released:
DOI: 10.2210/pdb4ifl/pdb
PDB entry 4ifl coloured by chain, front view.
PDB entry 4ifl coloured by chain, side view.
PDB entry 4ifl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structures of apo Keap1, Keap1-peptide, and Keap1-compound complexes
Pan H, Lin M, Yang Y, Callaway K, Baker J, Diep L, Yan J, Tanaka K, Zhu YL, Konradi AW, Jobling M, Tam D, Ren Z, Cheung H, Bova M, Riley BE, Yao N, Artis DR
To be published

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-171935 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Kelch-like ECH-associated protein 1 Chain: X
Molecule details ›
Chain: X
Length: 291 amino acids
Theoretical weight: 31.83 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
Nuclear factor erythroid 2-related factor 2 Chain: P
Molecule details ›
Chain: P
Length: 16 amino acids
Theoretical weight: 1.86 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q16236 (Residues: 69-84; Coverage: 3%)
Gene names: NFE2L2, NRF2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21212
Unit cell:
a: 77.499Å b: 92.03Å c: 46.158Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.19 0.235
Expression systems:
  • Escherichia coli
  • Not provided

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