1S5R: HBP1 SID-mSin3A PAH2 Complex

Solution Structure of HBP1 SID-mSin3A PAH2 Complex. Determined by solution NMR. Released 6 Jul 2004.

Method
Solution NMR
Organism
Mus musculus
Chains
2
Atoms
912
Mol. weight
12.92 kDa
Released
6 Jul 2004

Explore 1S5R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1S5R contains 5 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: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix366-37510
Chain B: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix303-31715
α-helix322-34524
α-helix355-36511
α-helix371-3799

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
high mobility group box transcription factor 1Aprotein23Q8R316 (AlphaFold model)
Sin3a proteinBprotein89Mus musculusQ60520 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1S5R_1 high mobility group box transcription factor 1 (chains A)
DFTPMDSSAVYVLSSMARQRRAS
Sequence of entity 2 (B), FASTA
>1S5R_2 Sin3a protein (chains B)
SLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALT
EQEVYAQVARLFKNQEDLLSEFGQFLPDA

Primary citation

HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations. Swanson, K.A., Knoepfler, P.S., Huang, K. et al. Nat Struct Mol Biol (2004) 11:738-746. DOI 10.1038/nsmb798 · PubMed

Other PDB entries of the same protein (UniProt Q8R316 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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