Structure analysis

Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain

X-ray diffraction
2.1Å 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
Accessible surface area: 23300 Å2
Buried surface area: 2400 Å2
Dissociation area: 450 Å2
Dissociation energy (ΔGdiss): -6 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -51 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B
Length: 255 amino acids
Theoretical weight: 28.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14653 (Residues: 173-427; Coverage: 60%)
Gene name: IRF3
Pfam: Interferon-regulatory factor 3
InterPro:
CATH: Tumour Suppressor Smad4
SCOP: Interferon regulatory factor 3 (IRF3), transactivation domain

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