PDBe 4yyh

X-ray diffraction
1.74Å resolution

Crystal structure of BRD9 Bromodomain bound to a crotonyllysine peptide

Released:

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 9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 108 amino acids
Theoretical weight: 12.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW Q9H8M2 (Residues: 134-239; Coverage: 18%)
Gene names: BRD9, UNQ3040/PRO9856
Sequence domains: Bromodomain
Structure domains: Bromodomain-like
Histone H4 Chains: Y, Z
Molecule details ›
Chains: Y, Z
Length: 11 amino acids
Theoretical weight: 1.11 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P62805 (Residues: 2-12; Coverage: 11%)
Gene names: H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 126.147Å b: 35.7Å c: 65.019Å
α: 90° β: 99.01° γ: 90°
R-values:
R R work R free
0.214 0.212 0.26
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided