1E91: Complex of the Mad1-Sin3B interaction domains

Structure of the complex of the Mad1-Sin3B interaction domains. Determined by solution NMR. Released 20 Nov 2000.

Method: Solution NMR
Organisms: MUS MUSCULUS, HOMO SAPIENS
Chains: 2
Atoms: 820
Mol. weight: 11.62 kDa
Released: 20 Nov 2000

Explore 1E91 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1E91 contains 6 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: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	5-20	16
α-helix	25-40	16
α-helix	55-65	11
α-helix	70-79	10
α-helix	81-82	2

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-12	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Paired amphipathic helix protein SIN3B	A	protein	85	MUS MUSCULUS	Q62141 (AlphaFold model)
Mad protein (max dimerizer)	B	protein	13	HOMO SAPIENS	Q05195 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1E91_1 PAIRED AMPHIPATHIC HELIX PROTEIN SIN3B (chains A)
ESDSVEFNNAISYVNKIKTRFLDHPEIYRSFLEILHTYQKEQLHTKGRPFRGMSEEEVFT
EVANLFRGQEDLLSEFGQFLPEAKR

Sequence of entity 2 (B), FASTA

>1E91_2 MAD PROTEIN (MAX DIMERIZER) (chains B)
NIQMLLEAADYLE

Primary citation

The MAD1-Sin3B Interaction Involves a Novel Helical Fold. Spronk, C.A.E.M., Tessari, M., Kaan, A.M. et al. Nat Struct Biol (2000) 7:1100-1104. DOI 10.1038/81944 · PubMed

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

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
2F05 Solution structure of free PAH2 domain of mSin3B
5Y95 Haddock model of mSIN3B PAH1 domain

Browse structure collections

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