› 5mgk

X-ray diffraction
2.3Å resolution

Crystal Structure of BAZ2A bromodomain in complex with 4-propionyl-pyrrole derivative 2

Released:
DOI: 10.2210/pdb5mgk/pdb
PDB 5mgk coloured by chain and viewed from the front.
PDB 5mgk coloured by chain and viewed from the side.
PDB 5mgk coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Discovery of BAZ2A bromodomain ligands.
Spiliotopoulos D, Wamhoff EC, Lolli G, Rademacher C, Caflisch A
Eur J Med Chem 139 564-572 (2017)
PMID: 28837921

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:
Bromodomain adjacent to zinc finger domain protein 2A Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 12.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UIF9 (Residues: 1796-1898; Coverage: 5%)
Gene names: BAZ2A, KIAA0314, TIP5
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

1 bound ligand:
Ligand 7MW 1 x 7MW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P3121
Unit cell:
a: 95.239Å b: 95.239Å c: 32.96Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.204 0.236
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Combined Protein- and Ligand-Observed NMR Workflow to Screen Fragment Cocktails against Multiple Proteins: A Case Study Using Bromodomains.
Johnson et al. (2020)
4 more