Research workbench
Solution NMR structures of the BRD3 et domain in complex with a CHD4 peptide
Analyse Solution NMR structures of the BRD3 et domain in complex with a CHD4 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BGG
- Type
- protein
- Length
- 100 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CHD4; Bromodomain-containing protein 3
- UniProt
- Q15059
Structure
solution nmr · 2 distinct chains · 48% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CHD4 | protein | 12 | 0% helix, 25% strand | — |
| B | Bromodomain-containing protein 3 | protein | 88 | 55% helix, 3% strand | Q15059 |
Interfaces
1 interface between chains.
- A–B · 506 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6BGG · Solution NMR structures of the BRD3 ET domain in complex with a CHD4 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q15059 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 3 (Q15059) · a predicted model of the same protein · chain B against A, TM-score 0.77
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 Q15059
- Elsewhere: RCSB PDB 6BGG · PDBe 6BGG · UniProt Q15059
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