2F05: Free PAH2 domain of mSin3B

Solution structure of free PAH2 domain of mSin3B. Determined by solution NMR. Released 28 Mar 2006.

Method: Solution NMR
Organism: Mus musculus
Chains: 1
Atoms: 713
Mol. weight: 12.24 kDa
Released: 28 Mar 2006

Explore 2F05 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F05 contains 5 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: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	5-20	16
α-helix	25-42	18
α-helix	55-65	11
α-helix	70-79	10
α-helix	82-84	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Paired amphipathic helix protein Sin3b	A	protein	105	Mus musculus	Q62141 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2F05_1 Paired amphipathic helix protein Sin3b (chains A)
ESDSVEFNNAISYVNKIKTRFLDHPEIYRSFLEILHTYQKEQLHTKGRPFRGMSEEEVFT
EVANLFRGQEDLLSEFGQFLPEAKRSLFTGNGSCEMNSGQKNEEK

Primary citation

Role of Structural and Dynamical Plasticity in Sin3: The Free PAH2 Domain is a Folded Module in mSin3B. van Ingen, H., Baltussen, M.A., Aelen, J. et al. J Mol Biol (2006) 358:485-497. DOI 10.1016/j.jmb.2006.01.100 · PubMed

Other PDB entries of the same protein (UniProt Q62141 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1E91 Structure of the complex of the Mad1-Sin3B interaction domains
1PD7 Extended SID of Mad1 bound to the PAH2 domain of mSin3B
2CR7 Solution structure of the first PAH domain of the mouse transcriptional repressor SIN3B
2CZY Solution structure of the NRSF/REST-mSin3B PAH1 complex
5Y95 Haddock model of mSIN3B PAH1 domain

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