Research workbench
NMR structure of the human MAD1 transrepression domain sid in complex with mammalian SIN3A PAH2 domain
Analyse NMR structure of the human MAD1 transrepression domain sid in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G1E
- Type
- protein
- Length
- 105 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q60520
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 16 | — | — |
| B | — | protein | 89 | — | Q60520 |
Compared structures
- 1G1E · NMR structure of the human MAD1 transrepression domain sid in complex with mammalian… · the same entry in another collection · chain A against A, TM-score 1.00
- Q60520 · AlphaFold monomer V2.0 prediction for paired amphipathic helix protein SIN3A (Q60520) · a predicted model of the same protein · chain B against A, TM-score 0.79
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q60520
- Elsewhere: RCSB PDB 1G1E · PDBe 1G1E · UniProt Q60520
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