Structure analysis

Atomic model of rabbit hemorrhagic disease virus

Electron Microscopy
6.5Å resolution
Assemblies composition:
homo 180-mer (preferred)
homo trimer
homo 15-mer
homo 18-mer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo 180-mer

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: homo trimer

Binding statistics and energies are not available for this assembly
Assembly 3
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Multimeric state: homo 15-mer

Binding statistics and energies are not available for this assembly
Assembly 4
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Multimeric state: homo 18-mer

Binding statistics and energies are not available for this assembly
Assembly 5
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Multimeric state: homo trimer
Accessible surface area: 67500 Å2
Buried surface area: 4800 Å2
Dissociation area: 1,600 Å2
Dissociation energy (ΔGdiss): 15 kcal/mol
Dissociation entropy (TΔSdiss): 15 kcal/mol
Interface energy (ΔGint): -35 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B, C
Length: 579 amino acids
Theoretical weight: 60.38 KDa
Source organism: Rabbit hemorrhagic disease virus
UniProt:
  • Canonical: F5BXG7 (Residues: 1766-2344; Coverage: 25%)
Pfam: Calicivirus coat protein
InterPro:

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