PDBe 3muk

X-ray diffraction
1.75Å resolution

Crystal structure of Brd4 bromodomain 1 with propionylated histone H3-K(prop)23

Released:
Source organisms:
Primary publication:
Interaction of propionylated and butyrylated histone H3 lysine marks with Brd4 bromodomains.
Angew. Chem. Int. Ed. Engl. 49 6768-72 (2010)
PMID: 20715035

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bromodomain-containing protein 4 Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 15.39 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ESU6 (Residues: 42-168; Coverage: 9%)
Gene names: Brd4, Mcap
Sequence domains: Bromodomain
Structure domains: Bromodomain-like
Histone H3.3 Chain: D
Molecule details ›
Chain: D
Length: 8 amino acids
Theoretical weight: 890 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P84243 (Residues: 22-29; Coverage: 6%)
Gene names: H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 35.213Å b: 47.008Å c: 78.101Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.219
Expression systems:
  • Escherichia coli
  • Not provided