Crystal structure of the first bromodomain of human BRD4 in complex with a diacetylated histone 4 peptide (H3K9AC/K14AC)

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 0% strand (DSSP).

Ligands and binding sites

• EDO · 1,2-ethanediol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• B–E · 481 Ų buried · 1 hydrogen bond · protein-protein
• A–D · 477 Ų buried · 1 hydrogen bond · protein-protein
• A–E · 197 Ų buried · 0 hydrogen bonds · protein-protein
• A–B · 67 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (acetylation, phosphorylation).

Compared structures

• 5NND · Crystal Structure of the first bromodomain of human BRD4 in complex with a diacetylated… · the same entry in another collection · chain E against E, TM-score 1.00
• O60885 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 4 (O60885) · a predicted model of the same protein · chain B against A, TM-score 0.98
• Q5TEC6 · AlphaFold monomer V2.0 prediction for histone HIST2H3PS2 (Q5TEC6) · a predicted model of the same protein · chain E against A, TM-score 0.51

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 Q5TEC6
• Elsewhere: RCSB PDB 5NND · PDBe 5NND · UniProt O60885 · UniProt Q5TEC6