PDBe 1u7v

X-ray diffraction
2.7Å resolution

Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mothers against decapentaplegic homolog 2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 198 amino acids
Theoretical weight: 22.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15796 (Residues: 270-467; Coverage: 42%)
Gene names: MADH2, MADR2, SMAD2
Sequence domains: MH2 domain
Structure domains: Tumour Suppressor Smad4
Mothers against decapentaplegic homolog 4 Chain: B
Molecule details ›
Chain: B
Length: 236 amino acids
Theoretical weight: 25.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13485 (Residues: 314-549; Coverage: 43%)
Gene names: DPC4, MADH4, SMAD4
Sequence domains: MH2 domain
Structure domains: Tumour Suppressor Smad4

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 49.24Å b: 59.951Å c: 207.418Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.243 0.279
Expression system: Escherichia coli