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Crystal structure of the first bromodomain of human BRD4 in complex with a diacetylated histone 4 peptide (H4K16ACK20AC)
Analyse Crystal structure of the first bromodomain of human BRD4 in complex with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UVY
- Type
- protein
- Length
- 119 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain-containing protein 4; Histone H4
- UniProt
- O60885, P62805
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain-containing protein 4 | protein | 109 | 62% helix, 0% strand | O60885 |
| B | Histone H4 | protein | 10 | 0% helix, 0% strand | P62805 |
Interfaces
1 interface between chains.
- A–B · 679 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (acetylation).
Compared structures
- 3UVY · Crystal Structure of the first bromodomain of human BRD4 in complex with a diacetylated… · 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 0.97
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
- Every structure of UniProt P62805
- Elsewhere: RCSB PDB 3UVY · PDBe 3UVY · UniProt O60885 · UniProt P62805
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