Structure analysis

A Dimerization-Dependent Mechanism Drives PRRSV NSP11 Functions As a Beta Interferon Antagonist and Endoribonuclease

X-ray diffraction
2.75Å resolution
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: 21000 Å2
Buried surface area: 1300 Å2
Dissociation area: 650 Å2
Dissociation energy (ΔGdiss): -2 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -9 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B
Length: 229 amino acids
Theoretical weight: 25.72 KDa
Source organism: Porcine reproductive and respiratory syndrome virus
Expression system: Escherichia coli
UniProt:
  • Canonical: E3V2B6 (Residues: 1085-1307; Coverage: 15%)
Pfam: Coronavirus replicase NSP15, uridylate-specific endoribonuclease
InterPro: Endoribonuclease EndoU-like

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