Structure analysis

Coiled-coil domain of human TRIM3

X-ray diffraction
3.8Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo dimer
Accessible surface area: 18647.8 Å2
Buried surface area: 9542.68 Å2
Dissociation area: 4,771.34 Å2
Dissociation energy (ΔGdiss): 80.42 kcal/mol
Dissociation entropy (TΔSdiss): 14.39 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-236922
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 17576.77 Å2
Buried surface area: 8864.56 Å2
Dissociation area: 4,276.25 Å2
Dissociation energy (ΔGdiss): 81.14 kcal/mol
Dissociation entropy (TΔSdiss): 14.08 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-236922

Macromolecules

Chains: A, B, C
Length: 319 amino acids
Theoretical weight: 34.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75382 (Residues: 7-322; Coverage: 43%)
Gene names: BERP, RNF22, RNF97, TRIM3
Pfam:

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