MolNFT v1 · #71974 · protein
Crystal structure of BRD4 bromodomain 1 with propionylated histone H3- K(PROP)23
3MUK · Bromodomain-containing protein 4: “Crystal structure of BRD4 bromodomain 1 with propionylated histone H3- K(PROP)23”. X-ray diffraction, 1 pocket (best druggability 0.27). MolNFT v1 #71974 on GenesisL1: 3D structure, binding sites…
- PDB
- 3MUK
- Type
- protein
- Length
- 134 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain-containing protein 4; Peptide of histone H3.3
- UniProt
- Q9ESU6, P84243
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain-containing protein 4 | protein | 127 | 52% helix, 0% strand | Q9ESU6 |
| D | Peptide of histone H3.3 | protein | 7 | 0% helix, 0% strand | P84243 |
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
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.27 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–D · 397 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 3MUK · Crystal structure of Brd4 bromodomain 1 with propionylated histone H3-K(prop)23 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ESU6 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 4 (Q9ESU6) · a predicted model of the same protein · chain A against A, TM-score 0.97
- P84243 · AlphaFold monomer V2.0 prediction for histone H3.3 (P84243) · a predicted model of the same protein · chain D against A, TM-score 0.50
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 Q9ESU6
- Every structure of UniProt P84243
- Elsewhere: RCSB PDB 3MUK · PDBe 3MUK · UniProt Q9ESU6 · UniProt P84243
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