› 6fmq

X-ray diffraction
2.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166724 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Kelch-like ECH-associated protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 414 amino acids
Theoretical weight: 45.85 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
ACY-SC1-GLU-THR-GLY-GLU-LEU Chain: D
Molecule details ›
Chain: D
Length: 7 amino acids
Theoretical weight: 786 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand EDO 4 x EDO
Ligand ACT 7 x ACT
Ligand NA 7 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 75.652Å b: 76.129Å c: 211.137Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.165 0.2
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

Recent advances in the development of protein-protein interactions modulators: mechanisms and clinical trials.
Lu et al. (2020)
5 more

2 mentions without citation

Modified Peptide Inhibitors of the Keap1-Nrf2 Protein-Protein Interaction Incorporating Unnatural Amino Acids.
Georgakopoulos et al. (2018)
1 more