› 7lak

X-ray diffraction
1.83Å resolution

Crystal structure of the first bromodomain (BD1) of human BRD2 bound to volasertib

Released:
DOI: 10.2210/pdb7lak/pdb
PDB entry 7lak coloured by chain, front view.
PDB entry 7lak coloured by chain, side view.
PDB entry 7lak coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Differential BET Bromodomain Inhibition by Dihydropteridinone and Pyrimidodiazepinone Kinase Inhibitors.
Karim RM, Bikowitz MJ, Chan A, Zhu JY, Grassie D, Becker A, Berndt N, Gunawan S, Lawrence NJ, Schönbrunn E
J Med Chem 64 15772-15786 (2021)
PMID: 34710325

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-150461 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bromodomain-containing protein 2 Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 14.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P25440 (Residues: 73-194; Coverage: 15%)
Gene names: BRD2, KIAA9001, RING3
Sequence domains: Bromodomain

Ligands and Environments

1 bound ligand:
Ligand IBI 1 x IBI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 55.89Å b: 81.5Å c: 48.18Å
α: 90° β: 138.74° γ: 90°
R-values:
R R work R free
0.17 0.168 0.212
Expression system: Escherichia coli

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Citations

3 citation in other articles

1,4-Dihydropyridinebutyrolactone-derived ring-opened ester and amide analogs targeting BET bromodomains.
Jiang et al. (2022)
2 more