1DEV: SMAD2 MH2 domain

Crystal structure of SMAD2 MH2 domain bound to the smad-binding domain of sara. Determined by X-ray diffraction at 2.2 Å resolution. Released 21 Jan 2000.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,643
Mol. weight: 52.82 kDa
Released: 21 Jan 2000

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

Secondary structure: helices and β-sheets

1DEV contains 25 α-helices and 36 β-strands across 4 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, 14 β-strands

Element	Residues	Length	Sheet
β-strand	264-267	4	1
β-strand	275-281	7	2
β-strand	284-285	2	2
β-strand	290-292	3	2
β-strand	296-300	5	3
α-helix	305-306	2
β-strand	307	1	3
β-strand	310-312	3	3
α-helix	323-332	10
β-strand	336-341	6	3
β-strand	344-349	6	3
β-strand	355-358	4	2
α-helix	360-366	7
β-strand	374-376	3	2
β-strand	381-385	5	3
α-helix	387-397	11
α-helix	398-400	3
α-helix	401-407	7
α-helix	408-412	5
β-strand	413-417	5	2
α-helix	431-433	3
β-strand	437-442	6	2
α-helix	443-454	12

Chain B: 3 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	677-679	3
β-strand	682	1	3
α-helix	686-690	5
α-helix	699-701	3
β-strand	702-705	4	1

Chain C: 10 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	263-264	2	4
α-helix	265	1
β-strand	267	1	5
β-strand	275-281	7	6
β-strand	284-285	2	6
α-helix	288-289	2
β-strand	290-292	3	6
β-strand	296-300	5	7
α-helix	305-306	2
β-strand	307	1	7
β-strand	310-312	3	7
α-helix	323-330	8
β-strand	336-341	6	7
β-strand	344-349	6	7
α-helix	354	1
β-strand	355-358	4	6
α-helix	360-366	7
β-strand	374-376	3	6
β-strand	381-385	5	7
α-helix	387-397	11
α-helix	402-406	5
α-helix	407-412	6
β-strand	413-417	5	6
β-strand	421	1	8
β-strand	430	1	8
β-strand	437-442	6	6
α-helix	443-454	12

Chain D: 3 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	677-679	3
β-strand	682	1	7
α-helix	686-690	5
α-helix	699-701	3
β-strand	702	1	5
β-strand	705-706	2	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MAD (mothers against decapentaplegic, Drosophila) homolog 2	A, C	protein	196	Homo sapiens	Q15796 (AlphaFold model)
Smad anchor for receptor activation	B, D	protein	41	Homo sapiens	O95405 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1DEV_1 MAD (mothers against decapentaplegic, Drosophila) homolog 2 (chains A, C)
LDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVN
RNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGC
NLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIEL
HLNGPLQWLDKVLTQM

Sequence of entity 2 (B, D), FASTA

>1DEV_2 Smad anchor for receptor activation (chains B, D)
SQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGV

Primary citation

Structural basis of Smad2 recognition by the Smad anchor for receptor activation. Wu, G., Chen, Y.G., Ozdamar, B. et al. Science (2000) 287:92-97. DOI 10.1126/science.287.5450.92 · PubMed

Other PDB entries of the same protein (UniProt Q15796 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6YIA 1.3 Å, 14-3-3 sigma in complex with SMAD2 pS465 peptide
6M64 1.45 Å, Crystal structure of SMAD2 in complex with CBP
1KHX 1.8 Å, Crystal structure of a phosphorylated Smad2
5XOD 1.85 Å, Crystal structure of human Smad2-Ski complex
6ZVQ 2.03 Å, Complex between SMAD2 MH2 domain and peptide from Ski corepressor
1U7V 2.7 Å, Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex
5ZOJ 2.79 Å, Crystal structure of human SMAD2-MAN1 complex
7CO1 3.3 Å, Crystal structure of SMAD2 in complex with wild-type CBP
2LB3 Structure of the WW domain of PIN1 in complex with a human phosphorylated Smad3 derived…

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