MolNFT v1 · #7258 · protein
NMR structure of the human MAD1 transrepression domain sid in complex with mammalian SIN3A PAH2 domain
1G1E: “NMR structure of the human MAD1 transrepression domain sid in complex with mammalian SIN3A PAH2 domain”. Solution nmr. MolNFT v1 #7258 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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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