› 5c87

X-ray diffraction
1.55Å resolution

Crystal structure of the human BRPF1 bromodomain in complex with SEED2

Released:
DOI: 10.2210/pdb5c87/pdb
PDB entry 5c87 coloured by chain, front view.
PDB entry 5c87 coloured by chain, side view.
PDB entry 5c87 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Twenty Crystal Structures of Bromodomain and PHD Finger Containing Protein 1 (BRPF1)/Ligand Complexes Reveal Conserved Binding Motifs and Rare Interactions.
Zhu J, Caflisch A
J Med Chem 59 5555-61 (2016)
PMID: 27167503

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157220 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peregrin Chain: A
Molecule details ›
Chain: A
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

Ligands and Environments

2 bound ligands:
Ligand NO3 1 x NO3
Ligand 4YS 1 x 4YS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P3221
Unit cell:
a: 60.559Å b: 60.559Å c: 63.599Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.182 0.198
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Ali et al. (2018)
2 more

1 mention without citation

Large-scale analysis of water stability in bromodomain binding pockets with grand canonical Monte Carlo.
Aldeghi et al. (2018)