9HZA: SMAD4 MH2, residues 272-552

SMAD4 MH2, residues 272-552. Determined by X-ray diffraction at 2.03 Å resolution. Released 22 Jul 2026.

Method: X-ray diffraction
Resolution: 2.03 Å
Organism: Homo sapiens
Chains: 3
Atoms: 5,636
Mol. weight: 94.71 kDa
Released: 22 Jul 2026

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

Secondary structure: helices and β-sheets

9HZA contains 30 α-helices and 39 β-strands across 3 chains. 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: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	288-291	4	1
α-helix	318-320	3
β-strand	322-330	9	1
β-strand	333-342	10	1
β-strand	347-351	5	2
β-strand	361-363	3	2
α-helix	374-380	7
β-strand	387-392	6	2
β-strand	396-401	6	2
β-strand	407-410	4	1
α-helix	412-418	7
α-helix	420-421	2
β-strand	426-429	4	1
β-strand	434-438	5	2
α-helix	440-456	17
α-helix	492-496	5
α-helix	497-499	3
β-strand	500-505	6	1
α-helix	518-520	3
β-strand	524-529	6	1
α-helix	530-542	13

Chain B: 11 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	288-291	4	3
α-helix	318-320	3
β-strand	322-330	9	3
β-strand	333-334	2	3
α-helix	337-338	2
β-strand	339-342	4	3
β-strand	347-351	5	4
β-strand	361-363	3	4
α-helix	374-381	8
β-strand	387-392	6	4
β-strand	396-401	6	4
β-strand	407-410	4	3
α-helix	412-418	7
α-helix	420-421	2
β-strand	426-429	4	3
β-strand	434-438	5	4
α-helix	440-465	26
β-strand	484	1	5
α-helix	492-495	4
α-helix	496-499	4
β-strand	500-505	6	3
α-helix	518-520	3
β-strand	524-529	6	3
α-helix	530-541	12
α-helix	544-545	2
β-strand	549	1	5

Chain C: 10 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	288-291	4	6
α-helix	318-320	3
β-strand	322-330	9	6
β-strand	333-342	10	6
β-strand	347-351	5	7
β-strand	361-363	3	7
α-helix	374-381	8
β-strand	387-392	6	7
β-strand	396-401	6	7
β-strand	407-410	4	6
α-helix	412-418	7
α-helix	420-421	2
β-strand	426-429	4	6
β-strand	434-438	5	7
α-helix	440-464	25
α-helix	492-495	4
α-helix	496-499	4
β-strand	500-505	6	6
α-helix	518-520	3
β-strand	524-529	6	6
α-helix	530-542	13
α-helix	544-545	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mothers against decapentaplegic homolog 4	A, B, C	protein	282	Homo sapiens	Q13485 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>9HZA_1 Mothers against decapentaplegic homolog 4 (chains A, B, C)
GRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFE
MDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLE
CKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQ
AATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWG
PDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD

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:

6YIC 1.6 Å, 14-3-3 sigma in complex with SMAD4 pS403 peptide
9HWE 1.7 Å, SMAD4 MH2, residues 314-552
5MEY 2.05 Å, Crystal structure of Smad4-MH1 bound to the GGCGC site.
1YGS 2.1 Å, Crystal structure of the SMAD4 tumor suppressor C-terminal domain
9QE6 2.1 Å, SMAD4 MH2 domain (residues 314-552) bound by Nanobody A1 (NbA1)
5UWU 2.24 Å, Crystal Structure of SMAD4 NES Peptide in complex with CRM1-Ran-RanBP1
1U7F 2.6 Å, Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex
5C4V 2.6 Å, Ski-like protein
1DD1 2.62 Å, Crystal structure analysis of the SMAD4 active fragment
1U7V 2.7 Å, Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex
1MR1 2.85 Å, Crystal Structure of a Smad4-Ski Complex
5MEZ 2.98 Å, Crystal structure of Smad4-MH1 bound to the GGCT site.

Browse structure collections

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