2N2H: Sds3

Solution structure of Sds3 in complex with Sin3A. Determined by solution NMR. Released 15 Jul 2015.

Method
Solution NMR
Organism
Mus musculus
Chains
2
Atoms
1,252
Mol. weight
17.82 kDa
Released
15 Jul 2015

Explore 2N2H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix211-2122
α-helix213-22311
Chain B: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix616-64126
α-helix646-6516
α-helix663-67311
α-helix675-6773
α-helix678-6858
α-helix689-71123
α-helix712-7165
α-helix717-7237

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Sin3 histone deacetylase corepressor complex component SDS3Aprotein27Mus musculusQ8BR65 (AlphaFold model)
Paired amphipathic helix protein Sin3aBprotein125Mus musculusQ60520 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2N2H_1 Sin3 histone deacetylase corepressor complex component SDS3 (chains A)
SNAAQLNYLLTDEQIMEDLRTLNKLKS
Sequence of entity 2 (B), FASTA
>2N2H_2 Paired amphipathic helix protein Sin3a (chains B)
SNAEHIYRCEDERFELDVVLETNLATIRVLEAIQKKLSRLSAEEQAKFRLDNTLGGTSEV
IHRKALQRIYADKAADIIDGLRKNPSIAVPIVLKRLKMKEEEWREAQRGFNKVWREQNEK
YYLKS

Primary citation

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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