2LD7: MSin3A PAH3-SAP30 SID complex

Solution structure of the mSin3A PAH3-SAP30 SID complex. Determined by solution NMR. Released 15 Jun 2011.

Method: Solution NMR
Organism: Mus musculus
Chains: 2
Atoms: 1,356
Mol. weight: 19.22 kDa
Released: 15 Jun 2011

Explore 2LD7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2LD7 contains 9 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: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	146-148	3
α-helix	155-164	10
α-helix	175-186	12
α-helix	193-206	14

Chain B: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	463-475	13
α-helix	478-492	15
α-helix	498-504	7
α-helix	506-509	4
α-helix	513-523	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone deacetylase complex subunit SAP30	A	protein	94	Mus musculus	O88574 (AlphaFold model)
Paired amphipathic helix protein Sin3a	B	protein	75	Mus musculus	Q60520 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2LD7_1 Histone deacetylase complex subunit SAP30 (chains A)
SNAGSDDDGGDSPVQDIDTPEVDLYQLQVNTLRRYKRHFKLPTRPGLNKAQLVEIVGCHF
KSIPVNEKDTLTCFIYSVRNDKNKSDLKADSGVH

Sequence of entity 2 (B), FASTA

>2LD7_2 Paired amphipathic helix protein Sin3a (chains B)
SNASKHGVGTESLFFDKVRKALRSAEAYENFLRCLVIFNQEVISRAELVQLVSPFLGKFP
ELFNWFKNFLGYKES

Primary citation

Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding. Xie, T., He, Y., Korkeamaki, H. et al. J Biol Chem (2011) 286:27814-27824. DOI 10.1074/jbc.M111.252494 · PubMed

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