› 7mr9

X-ray diffraction
1.19Å resolution

Crystal structure of the first bromodomain (BD1) of human BRD4 bound to NC-II-153

Released:
DOI: 10.2210/pdb7mr9/pdb
PDB 7mr9 coloured by chain and viewed from the front.
PDB 7mr9 coloured by chain and viewed from the side.
PDB 7mr9 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Bivalent BET Bromodomain Inhibitors Confer Increased Potency and Selectivity for BRDT via Protein Conformational Plasticity.
Guan X, Cheryala N, Karim RM, Chan A, Berndt N, Qi J, Georg GI, Schönbrunn E
J Med Chem (2022)
PMID: 35867655

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bromodomain-containing protein 4 Chain: A
Molecule details ›
Chain: A
Length: 127 amino acids
Theoretical weight: 15.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O60885 (Residues: 44-168; Coverage: 9%)
Gene names: BRD4, HUNK1
Sequence domains: Bromodomain

Ligands and Environments

2 bound ligands:
Ligand ZMM 1 x ZMM
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 37.44Å b: 44.31Å c: 77.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 0.185
Expression system: Escherichia coli BL21(DE3)

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