› 5o5h

X-ray diffraction
1.85Å resolution

Crystal structure of the human BRPF1 bromodomain in complex with BZ053

Released:
DOI: 10.2210/pdb5o5h/pdb
PDB 5o5h coloured by chain and viewed from the front.
PDB 5o5h coloured by chain and viewed from the side.
PDB 5o5h coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structure-based discovery of selective BRPF1 bromodomain inhibitors.
Zhu J, Zhou C, Caflisch A
Eur J Med Chem 155 337-352 (2018)
PMID: 29902720

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)
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

Ligands and Environments

2 bound ligands:
Ligand 9LK 2 x 9LK
Ligand NO3 1 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P3221
Unit cell:
a: 61.027Å b: 61.027Å c: 63.787Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.19 0.235
Expression system: Escherichia coli

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Citations

2 review citations

Functional Roles of Bromodomain Proteins in Cancer.
Boyson et al. (2021)
1 more