2RMS: MSin3A PAH1-SAP25 SID complex

Solution structure of the mSin3A PAH1-SAP25 SID complex. Determined by solution NMR. Released 22 Jan 2008.

Method
Solution NMR
Organism
Mus musculus
Chains
2
Atoms
995
Mol. weight
14.23 kDa
Released
22 Jan 2008

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

Secondary structure: helices and β-sheets

2RMS contains 6 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: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix123-13614
α-helix137-1393
α-helix141-15616
α-helix161-17111
α-helix176-1827
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix132-14413

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Paired amphipathic helix protein Sin3aAprotein71Mus musculusQ60520 (AlphaFold model)
MSin3A-binding proteinBprotein61Mus musculusQ1EHW4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2RMS_1 Paired amphipathic helix protein Sin3a (chains A)
QRLKVEDALSYLDQVKLQFGSQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPDL
IMGFNTFLPPG
Sequence of entity 2 (B), FASTA
>2RMS_2 MSin3A-binding protein (chains B)
SSTWLSEAEMIALAGLLQMSQGEQTPNCVASSLPSTSCPDPVSVSEDPGPSGDQSCSGTD
T

Primary citation

Conserved Themes in Target Recognition by the PAH1 and PAH2 Domains of the Sin3 Transcriptional Corepressor. Sahu, S.C., Swanson, K.A., Kang, R.S. et al. J Mol Biol (2007) 375:1444-1456. DOI 10.1016/j.jmb.2007.11.079 · PubMed

Other PDB entries of the same protein (UniProt Q60520 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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