Structure analysis

crystal structure of the KEAP1-NEH2 complex

X-ray diffraction
2.2Å resolution
Source organism: Homo sapiens
Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 11900 Å2
Buried surface area: 1600 Å2
Dissociation area: 400 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 6 kcal/mol
Interface energy (ΔGint): -2 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: monomeric

Binding statistics and energies are not available for this assembly

Macromolecules

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
Pfam: Kelch motif
InterPro:
CATH: Kelch-type beta propeller

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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

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