1dd1

X-ray diffraction
2.62Å resolution

CRYSTAL STRUCTURE ANALYSIS OF THE SMAD4 ACTIVE FRAGMENT

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of a transcriptionally active Smad4 fragment.
Structure 7 1493-503 (1999)
PMID: 10647180

Function and Biology Details

Biochemical function:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
PDBe Complex ID:
PDB-CPX-171713 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mothers against decapentaplegic homolog 4 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 268 amino acids
Theoretical weight: 29.42 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q13485 (Residues: 285-552; Coverage: 49%)
Gene names: DPC4, MADH4, SMAD4
Sequence domains: MH2 domain
Structure domains: Tumour Suppressor Smad4

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I4122
Unit cell:
a: 142.433Å b: 142.433Å c: 195.478Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.175