6M64: SMAD2

Crystal structure of SMAD2 in complex with CBP. Determined by X-ray diffraction at 1.45 Å resolution. Released 25 Nov 2020.

Method: X-ray diffraction
Resolution: 1.45 Å
Organism: Homo sapiens
Chains: 6
Atoms: 5,863
Mol. weight: 79.81 kDa
Released: 25 Nov 2020

Explore 6M64 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6M64 contains 30 α-helices and 36 β-strands across 6 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.

Chains A and E: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	275-281	7	1
β-strand	284-285	2	1
α-helix	288-289	2
β-strand	290-292	3	1
β-strand	296-300	5	2
β-strand	310-312	3	2
α-helix	313-315	3
α-helix	323-332	10
β-strand	336-341	6	2
β-strand	344-349	6	2
β-strand	355-358	4	1
α-helix	360-366	7
β-strand	374-376	3	1
β-strand	381-386	6	2
α-helix	387-398	12
α-helix	402-406	5
α-helix	407-412	6
β-strand	413-418	6	1
α-helix	431-433	3
β-strand	437-442	6	1
α-helix	443-453	11

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1953-1967	15

Chain C: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	275-281	7	3
β-strand	284-285	2	3
α-helix	288-289	2
β-strand	290-292	3	3
β-strand	296-300	5	4
β-strand	310-312	3	4
α-helix	313-315	3
α-helix	323-332	10
β-strand	336-341	6	4
β-strand	344-349	6	4
β-strand	355-358	4	3
α-helix	360-366	7
β-strand	374-376	3	3
β-strand	381-386	6	4
α-helix	387-400	14
α-helix	402-406	5
α-helix	407-412	6
β-strand	413-418	6	3
α-helix	431-433	3
β-strand	437-442	6	3
α-helix	443-453	11

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1953-1968	16

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1953-1969	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mothers against decapentaplegic homolog 2	A, C, E	protein	208	Homo sapiens	Q15796 (AlphaFold model)
CBP	B, D, F	protein	28	Homo sapiens	Q92793 (AlphaFold model)

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

>6M64_1 Mothers against decapentaplegic homolog 2 (chains A, C, E)
GPDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNV
NRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPG
CNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIE
LHLNGPLQWLDKVLTQMGSPSVRCSEME

Sequence of entity 2 (B, D, F), FASTA

>6M64_2 CBP (chains B, D, F)
GPPPAAVEAARQILREAQQQQHLYSDED

Primary citation

Structural basis for transcriptional coactivator recognition by SMAD2 in TGF-beta signaling. Miyazono, K.I., Ito, T., Fukatsu, Y. et al. Sci Signal (2020) 13. DOI 10.1126/scisignal.abb9043 · 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
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
1DEV 2.2 Å, Crystal structure of SMAD2 MH2 domain bound to the smad-binding domain of sara
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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