1DD1: SMAD4

Crystal structure analysis of the SMAD4 active fragment. Determined by X-ray diffraction at 2.62 Å resolution. Released 27 Nov 1999.

Method: X-ray diffraction
Resolution: 2.62 Å
Organism: Homo sapiens
Chains: 3
Atoms: 5,889
Mol. weight: 89.12 kDa
Released: 27 Nov 1999

Explore 1DD1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DD1 contains 31 α-helices and 43 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: 10 helices, 13 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	333-334	2	1
α-helix	337-338	2
β-strand	339-342	4	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
β-strand	426-429	4	1
α-helix	430	1
β-strand	434-438	5	2
α-helix	440-454	15
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	374-380	7
β-strand	387-392	6	4
β-strand	396-401	6	4
β-strand	407-410	4	3
α-helix	412-417	6
α-helix	420-421	2
β-strand	426-429	4	3
β-strand	434-438	5	4
α-helix	440-464	25
β-strand	483-484	2	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	530-540	11
α-helix	544-545	2
β-strand	549-550	2	5

Chain C: 10 helices, 15 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	333-334	2	6
α-helix	337-338	2
β-strand	339-342	4	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
β-strand	426-429	4	6
α-helix	430	1
β-strand	434-438	5	7
α-helix	440-465	26
β-strand	483-484	2	8
α-helix	492-497	6
β-strand	500-505	6	6
α-helix	518-520	3
β-strand	524-529	6	6
α-helix	530-541	12
α-helix	544-545	2
β-strand	549-550	2	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SMAD4	A, B, C	protein	268	Homo sapiens	Q13485 (AlphaFold model)

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

>1DD1_1 SMAD4 (chains A, B, C)
NGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSS
CPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSD
HAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAA
VAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCW
IEIHLHRALQLLDEVLHTMPIADPQPLD

Primary citation

Crystal structure of a transcriptionally active Smad4 fragment. Qin, B., Lam, S.S., Lin, K. Structure (1999) 7:1493-1503. DOI 10.1016/S0969-2126(00)88340-9 · PubMed

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
9HZA 2.03 Å, SMAD4 MH2, residues 272-552
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
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.

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