Crystal structure of the human BRPF1 bromodomain in complex with BZ054

Structure

x-ray diffraction · 3 distinct chains · 64% helix, 0% strand (DSSP).

Ligands and binding sites

• B0H · ~{N}-[4-[[(3~{S},5~{R})-3,5-dimethylpiperidin-1-yl]methyl]-1,3-thiazol-2-yl]-2,4-dimethyl-1,3-oxazole-5-carboxamide · ligand · 3 copies · chains A, B, C, D

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

Pockets

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

Interfaces

5 interfaces between chains.

• A–B · 550 Ų buried · 6 hydrogen bonds · protein-protein
• B–C · 430 Ų buried · 3 hydrogen bonds · protein-protein
• C–D · 189 Ų buried · 2 hydrogen bonds · protein-protein
• A–C · 127 Ų buried · 3 hydrogen bonds · protein-protein
• A–D · 19 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 5OWA · Crystal structure of the human BRPF1 bromodomain in complex with BZ054 · the same entry in another collection · chain D against D, TM-score 1.00
• P55201 · AlphaFold monomer V2.0 prediction for peregrin (P55201) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P55201
• Elsewhere: RCSB PDB 5OWA · PDBe 5OWA · UniProt P55201