Structure analysis

Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1

X-ray diffraction
2.89Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 11100 Å2
Buried surface area: 4200 Å2
Dissociation area: 2,100 Å2
Dissociation energy (ΔGdiss): 33 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -41 kcal/mol
Symmetry number: 2

Macromolecules

Chains: A, B, C, D
Length: 103 amino acids
Theoretical weight: 12.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q32MZ4 (Residues: 162-249; Coverage: 11%)
  • Best match: Q32MZ4-4 (Residues: 290-377)
Gene names: GCF2, LRRFIP1, TRIP
InterPro: Leucine-rich repeat flightless-interacting protein 1/2
CATH: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

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