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Crystal structure of the first bromodomain of human BRD4 in complex with an acetylated BAZ1B peptide (K221AC)
Analyse Crystal structure of the first bromodomain of human BRD4 in complex with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NNF
- Type
- protein
- Length
- 134 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain-containing protein 4; FLPH(ALY)YDVKL
- UniProt
- O60885
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain-containing protein 4 | protein | 126 | 52% helix, 0% strand | O60885 |
| B | FLPH(ALY)YDVKL | protein | 8 | 38% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 599 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 5NNF · Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated… · the same entry in another collection · chain A against A, TM-score 1.00
- O60885 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 4 (O60885) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 O60885
- Elsewhere: RCSB PDB 5NNF · PDBe 5NNF · UniProt O60885
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