5ffv

X-ray diffraction
1.3Å resolution

Crystal structure of the bromodomain of human BRPF1 in complex with H3K14ac histone peptide

Released:
Source organism: Homo sapiens
Entry authors: Tallant C, Nunez-Alonso G, Savitsky P, Krojer T, von Delft F, Arrowsmith CH, Edwards AM, Bountra C, Knapp S

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-157222 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peregrin Chains: A, B
Molecule details ›
Chains: A, B
Length: 116 amino acids
Theoretical weight: 13.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55201 (Residues: 626-740; Coverage: 10%)
Gene names: BR140, BRPF1
Sequence domains: Bromodomain
Structure domains: Bromodomain-like
Histone H3.1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 11 amino acids
Theoretical weight: 1.2 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 10-20; Coverage: 8%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21212
Unit cell:
a: 74.266Å b: 74.354Å c: 49.509Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.206
Expression systems:
  • Escherichia coli
  • Not provided