Structure analysis

Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex

X-ray diffraction
2.6Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 24918.81 Å2
Buried surface area: 6785.13 Å2
Dissociation area: 2,175.35 Å2
Dissociation energy (ΔGdiss): 15.63 kcal/mol
Dissociation entropy (TΔSdiss): 13.37 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-160786
Complex Portal ID: CPX-3252

Macromolecules

Chains: A, C
Length: 198 amino acids
Theoretical weight: 22.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P84022 (Residues: 228-425; Coverage: 47%)
Gene names: MADH3, SMAD3
Pfam: MH2 domain
InterPro:
CATH: Tumour Suppressor Smad4
SCOP: SMAD domain

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Chain: B
Length: 239 amino acids
Theoretical weight: 26.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13485 (Residues: 314-552; Coverage: 43%)
Gene names: DPC4, MADH4, SMAD4
Pfam: MH2 domain
InterPro:
CATH: Tumour Suppressor Smad4
SCOP: SMAD domain

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