› 5erc

X-ray diffraction
2.05Å resolution

X-ray crystal structure of BRPF1 PZP domain

Released:
DOI: 10.2210/pdb5erc/pdb
PDB entry 5erc coloured by chain, front view.
PDB entry 5erc coloured by chain, side view.
PDB entry 5erc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation.
Klein BJ, Muthurajan UM, Lalonde ME, Gibson MD, Andrews FH, Hepler M, Machida S, Yan K, Kurumizaka H, Poirier MG, Côté J, Luger K, Kutateladze TG
OpenAccess logo Nucleic Acids Res 44 472-84 (2016)
PMID: 26626149

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-547548 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peregrin Chain: A
Molecule details ›
Chain: A
Length: 177 amino acids
Theoretical weight: 19.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55201 (Residues: 274-450; Coverage: 15%)
Gene names: BR140, BRPF1
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 5 x ZN
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P6122
Unit cell:
a: 73.87Å b: 73.87Å c: 147.13Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.162 0.193
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Functions of bromodomain-containing proteins and their roles in homeostasis and cancer.
Fujisawa et al. (2017)
11 more

6 mentions without citation

Insights into newly discovered marks and readers of epigenetic information.
Andrews et al. (2016)
5 more