› 5l97

X-ray diffraction
2.05Å resolution

Crystal Structure of BAZ2B bromodomain in complex with 3-amino-2-methylpyridine derivative 3

Released:
DOI: 10.2210/pdb5l97/pdb
PDB 5l97 coloured by chain and viewed from the front.
PDB 5l97 coloured by chain and viewed from the side.
PDB 5l97 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Derivatives of 3-amino-2-methylpyridine as BAZ2B Bromodomain Ligands: in silico Discovery and in crystallo Validation.
Marchand JR, Lolli G, Caflisch A
J. Med. Chem. (2016)
PMID: 27731638

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 2B Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 13.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UIF8 (Residues: 2054-2167; Coverage: 5%)
Gene names: BAZ2B, KIAA1476
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

1 bound ligand:
Ligand 6RW 1 x 6RW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2221
Unit cell:
a: 81.807Å b: 96.716Å c: 57.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.211
Expression system: Escherichia coli

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Citations

9 citation in other articles

Discovery of BAZ2A bromodomain ligands.
Spiliotopoulos et al. (2017)
8 more