Solution structure of Sds3 in complex with Sin3A. Determined by solution NMR. Released 15 Jul 2015.
Explore 2N2H in 3D Show helices and sheets RCSB PDB PDBe
2N2H contains 10 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 | 211-212 | 2 | |
| α-helix | 213-223 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 616-641 | 26 | |
| α-helix | 646-651 | 6 | |
| α-helix | 663-673 | 11 | |
| α-helix | 675-677 | 3 | |
| α-helix | 678-685 | 8 | |
| α-helix | 689-711 | 23 | |
| α-helix | 712-716 | 5 | |
| α-helix | 717-723 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sin3 histone deacetylase corepressor complex component SDS3 | A | protein | 27 | Mus musculus | Q8BR65 (AlphaFold model) |
| Paired amphipathic helix protein Sin3a | B | protein | 125 | Mus musculus | Q60520 (AlphaFold model) |
>2N2H_1 Sin3 histone deacetylase corepressor complex component SDS3 (chains A) SNAAQLNYLLTDEQIMEDLRTLNKLKS
>2N2H_2 Paired amphipathic helix protein Sin3a (chains B) SNAEHIYRCEDERFELDVVLETNLATIRVLEAIQKKLSRLSAEEQAKFRLDNTLGGTSEV IHRKALQRIYADKAADIIDGLRKNPSIAVPIVLKRLKMKEEEWREAQRGFNKVWREQNEK YYLKS
Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepressor complex. Clark, M.D., Marcum, R., Graveline, R. et al. Proc Natl Acad Sci U S A (2015) 112:E3669-E3678. DOI 10.1073/pnas.1504021112 · PubMed
Other PDB entries of the same protein (UniProt Q8BR65 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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