› 1khu

X-ray diffraction
2.5Å resolution

Smad1 crystal structure reveals the details of BMP signaling pathway

Released:
DOI: 10.2210/pdb1khu/pdb
PDB entry 1khu coloured by chain, front view.
PDB entry 1khu coloured by chain, side view.
PDB entry 1khu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of Smad1 activation by receptor kinase phosphorylation.
Qin BY, Chacko BM, Lam SS, de Caestecker MP, Correia JJ, Lin K
Mol Cell 8 1303-12 (2001)
PMID: 11779505

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172411 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mothers against decapentaplegic homolog 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 218 amino acids
Theoretical weight: 24.55 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q15797 (Residues: 248-465; Coverage: 47%)
Gene names: BSP1, MADH1, MADR1, SMAD1
Sequence domains: MH2 domain
Structure domains: Tumour Suppressor Smad4

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: R3
Unit cell:
a: 138.129Å b: 138.129Å c: 199.34Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.239 0.274

Quick links

Citations

17 review citations

Mechanisms of TGF-beta signaling from cell membrane to the nucleus.
Shi et al. (2003)
16 more

9 mentions without citation

Phosphorylation in protein-protein binding: effect on stability and function.
Nishi et al. (2011)
8 more