9HWE: SMAD4 MH2, residues 314-552

SMAD4 MH2, residues 314-552. Determined by X-ray diffraction at 1.7 Å resolution. Released 15 Jul 2026.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
1
Atoms
1,712
Mol. weight
26.5 kDa
Released
15 Jul 2026

Explore 9HWE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9HWE contains 7 α-helices and 11 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 7 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand322-33091
β-strand333-342101
β-strand347-35152
β-strand361-36332
α-helix374-3807
β-strand387-39262
β-strand396-40162
β-strand407-41041
α-helix412-4176
α-helix420-4212
β-strand427-42931
β-strand434-43852
α-helix440-45617
α-helix492-4976
β-strand500-50451
α-helix518-5203
β-strand524-52961
α-helix530-54213

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Mothers against decapentaplegic homolog 4Aprotein240Homo sapiensQ13485 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9HWE_1 Mothers against decapentaplegic homolog 4 (chains A)
GISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHR
TEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPS
AYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGV
DDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD

Primary citation

(RUNNING TITLE:) Insights into the structure-activity relationship of SMAD4 variants linked to Myhre syndrome and hereditary hemorrhagic telangiectasia. Torner, C., Condeminas, M., Pluta, R. et al. To be published.

Other PDB entries of the same protein (UniProt Q13485 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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