Structure analysis

X-ray crystal structure of IRF-3 and its functional implications

X-ray diffraction
2.3Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10976.96 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-172049
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 11818.34 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-172049

Macromolecules

Chains: A, B
Length: 258 amino acids
Theoretical weight: 28.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14653 (Residues: 175-427; Coverage: 59%)
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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