Structure analysis

D domain of b-TrCP

X-ray diffraction
2.5Å 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: 6067.43 Å2
Buried surface area: 4066.67 Å2
Dissociation area: 1,989.41 Å2
Dissociation energy (ΔGdiss): 35.59 kcal/mol
Dissociation entropy (TΔSdiss): 10.84 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-195122

Macromolecules

Chains: A, B
Length: 52 amino acids
Theoretical weight: 6.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9Y297 (Residues: 128-177; Coverage: 8%)
Gene names: BTRC, BTRCP, FBW1A, FBXW1A
Pfam: D domain of beta-TrCP
InterPro: D domain of beta-TrCP
CATH: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

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