Research workbench
Solution structure of the NRSF/REST-MSIN3B PAH1 complex
Analyse Solution structure of the NRSF/REST-MSIN3B PAH1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CZY
- Type
- protein
- Length
- 92 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Paired amphipathic helix protein SIN3B; Transcription factor rest (version 3)
- UniProt
- Q62141, Q13127
Structure
solution nmr · 2 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Paired amphipathic helix protein SIN3B | protein | 77 | 62% helix, 0% strand | Q62141 |
| B | Transcription factor rest (version 3) | protein | 15 | 80% helix, 0% strand | Q13127 |
Interfaces
1 interface between chains.
- A–B · 691 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2CZY · Solution structure of the NRSF/REST-mSin3B PAH1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q62141 · AlphaFold monomer V2.0 prediction for paired amphipathic helix protein SIN3B (Q62141) · a predicted model of the same protein · chain A against A, TM-score 0.86
- Q13127 · AlphaFold monomer V2.0 prediction for RE1-silencing transcription factor (Q13127) · a predicted model of the same protein · chain B against A, TM-score 0.69
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 Q62141
- Every structure of UniProt Q13127
- Elsewhere: RCSB PDB 2CZY · PDBe 2CZY · UniProt Q62141 · UniProt Q13127
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.