1G1E: Human MAD1 transrepression domain sid

NMR structure of the human MAD1 transrepression domain sid in complex with mammalian SIN3A PAH2 domain. Determined by solution NMR. Released 6 Dec 2000.

Method: Solution NMR
Organism: Mus musculus
Chains: 2
Atoms: 869
Mol. weight: 12.31 kDa
Released: 6 Dec 2000

Explore 1G1E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G1E 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	8-20	13

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	302-317	16
α-helix	322-344	23
α-helix	355-365	11
α-helix	370-377	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MAD1 protein	A	protein	16		Q05195 (AlphaFold model)
SIN3A	B	protein	89	Mus musculus	Q60520 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1G1E_1 MAD1 PROTEIN (chains A)
RMNIQMLLEAADYLER

Sequence of entity 2 (B), FASTA

>1G1E_2 SIN3A (chains B)
SLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALT
EQEVYAQVARLFKNQEDLLSEFGQFLPDA

Primary citation

Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex. Brubaker, K., Cowley, S.M., Huang, K. et al. Cell (2000) 103:655-665. DOI 10.1016/S0092-8674(00)00168-9 · 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
1PD7 Extended SID of Mad1 bound to the PAH2 domain of mSin3B
1S5Q Solution Structure of Mad1 SID-mSin3A PAH2 Complex

Browse structure collections

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