Structure analysis

Crystal structures of K63-linked di- and tri-ubiquitin reveal a highly extended chain architecture

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

Assemblies

Assembly 1
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Multimeric state: homo dimer
Accessible surface area: 9057.46 Å2
Buried surface area: 1058.14 Å2
Dissociation area: 115.19 Å2
Dissociation energy (ΔGdiss): -2.11 kcal/mol
Dissociation entropy (TΔSdiss): 9.63 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-143418
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 4806.33 Å2
Buried surface area: 427.86 Å2
Dissociation area: 12.42 Å2
Dissociation energy (ΔGdiss): 5.51 kcal/mol
Dissociation entropy (TΔSdiss): -0.24 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-143327
Assembly 3 (preferred)
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Multimeric state: monomeric
Accessible surface area: 4548.79 Å2
Buried surface area: 332.62 Å2
Dissociation area: 33.16 Å2
Dissociation energy (ΔGdiss): 15.2 kcal/mol
Dissociation entropy (TΔSdiss): -0.23 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-143327

Macromolecules

Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Pfam: Ubiquitin family
InterPro:
CATH: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

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