1S5Q: Mad1 SID-mSin3A PAH2 Complex

Solution Structure of Mad1 SID-mSin3A PAH2 Complex. Determined by solution NMR. Released 6 Jul 2004.

Method: Solution NMR
Organism: Mus musculus
Chains: 2
Atoms: 869
Mol. weight: 12.31 kDa
Released: 6 Jul 2004

Explore 1S5Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1S5Q 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

Element	Residues	Length	Sheet
α-helix	10-20	11

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	301-317	17
α-helix	322-344	23
α-helix	355-365	11
α-helix	370-379	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MAD protein	A	protein	16		Q05195 (AlphaFold model)
Sin3a protein	B	protein	89	Mus musculus	Q60520 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1S5Q_1 MAD protein (chains A)
RMNIQMLLEAADYLER

Sequence of entity 2 (B), FASTA

>1S5Q_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 Q05195 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1NLW 2.0 Å, Crystal structure of Mad-Max recognizing DNA
1E91 Structure of the complex of the Mad1-Sin3B interaction domains
1G1E NMR structure of the human MAD1 transrepression domain sid in complex with mammalian…
1PD7 Extended SID of Mad1 bound to the PAH2 domain of mSin3B

Browse structure collections

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