2RMR: MSin3A PAH1 domain

Name: PDB 2RMR: Solution structure of mSin3A PAH1 domain
Published: 2008-01-22
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

Solution structure of mSin3A PAH1 domain. Determined by solution NMR. Released 22 Jan 2008.

Method: Solution NMR
Organism: Mus musculus
Chains: 1
Atoms: 570
Mol. weight: 8.08 kDa
Released: 22 Jan 2008

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

Secondary structure: helices and β-sheets

2RMR contains 4 α-helices and 0 β-strands across 1 chain. 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: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	126-136	11
α-helix	141-155	15
α-helix	161-171	11
α-helix	176-183	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Paired amphipathic helix protein Sin3a	A	protein	71	Mus musculus	Q60520 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2RMR_1 Paired amphipathic helix protein Sin3a (chains A)
QRLKVEDALSYLDQVKLQFGSQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPDL
IMGFNTFLPPG

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:

1G1E NMR structure of the human MAD1 transrepression domain sid in complex with mammalian…
1S5Q Solution Structure of Mad1 SID-mSin3A PAH2 Complex
1S5R Solution Structure of HBP1 SID-mSin3A PAH2 Complex
2L9S Solution structure of Pf1 SID1-mSin3A PAH2 Complex
2LD7 Solution structure of the mSin3A PAH3-SAP30 SID complex
2N2H Solution structure of Sds3 in complex with Sin3A
2RMS Solution structure of the mSin3A PAH1-SAP25 SID complex

Browse structure collections

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