Solution structure of the coiled-coil complex between MBD2 and p66alpha. Determined by solution NMR. Released 4 May 2011.
Explore 2L2L in 3D Show helices and sheets RCSB PDB PDBe
2L2L contains 2 α-helices and 0 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 138-168 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 217-239 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcriptional repressor p66-alpha | A | protein | 43 | Homo sapiens | Q86YP4 (AlphaFold model) |
| Methyl-CpG-binding domain protein 2 | B | protein | 36 | Homo sapiens | Q9UBB5 (AlphaFold model) |
>2L2L_1 Transcriptional repressor p66-alpha (chains A) GSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQK
>2L2L_2 Methyl-CpG-binding domain protein 2 (chains B) GSKAFIVTDEDIRKQEERVQQVRKKLEEALMADILS
p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2-NuRD complex. Gnanapragasam, M.N., Scarsdale, J.N., Amaya, M.L. et al. Proc Natl Acad Sci U S A (2011) 108:7487-7492. DOI 10.1073/pnas.1015341108 · PubMed
Other PDB entries of the same protein (UniProt Q86YP4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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