Structure analysis

Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein

X-ray diffraction
1.2Å resolution
Source organism: Homo sapiens
Assemblies composition:
homo dimer (preferred)
homo hexamer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 6300 Å2
Buried surface area: 1700 Å2
Dissociation area: 850 Å2
Dissociation energy (ΔGdiss): 4 kcal/mol
Dissociation entropy (TΔSdiss): 10 kcal/mol
Interface energy (ΔGint): -1 kcal/mol
Symmetry number: 2
Assembly 3
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Multimeric state: homo hexamer

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B, C
Length: 50 amino acids
Theoretical weight: 5.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HB71 (Residues: 1-47; Coverage: 21%)
Gene names: CACYBP, PNAS-107, S100A6BP, SIP
InterPro:
CATH: UVR domain
SCOP: Siah interacting protein N terminal domain-like

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