4QB3: First bromodomain of human BRD4

Crystal structure of the first bromodomain of human BRD4 in complex with Olinone. Determined by X-ray diffraction at 0.94 Å resolution. Released 22 Apr 2015.

Method
X-ray diffraction
Resolution
0.94 Å
Organism
Homo sapiens
Chains
1
Atoms
1,383
Mol. weight
15.46 kDa
Ligands
30M
Released
22 Apr 2015

Explore 4QB3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QB3 contains 11 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix43-497
α-helix61-655
α-helix66-716
α-helix72-754
α-helix81-833
α-helix97-1004
α-helix107-1159
α-helix122-13918
α-helix1411
α-helix145-16117
α-helix164-1674

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bromodomain-containing protein 4Aprotein127Homo sapiensO60885 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4QB3_1 Bromodomain-containing protein 4 (chains A)
SMNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKII
KTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKI
NELPTEE

Ligands and cofactors

IDNameFormulaCopies
30MN-[4-(1-oxo-1,2,3,4-tetrahydro-5H-pyrido[4,3-b]indol-5-yl)butyl]acetamideC17 H21 N3 O21

Water and common crystallization additives (EDO) are not listed.

Primary citation

Selective chemical modulation of gene transcription favors oligodendrocyte lineage progression. Gacias, M., Gerona-Navarro, G., Plotnikov, A.N. et al. Chem Biol (2014) 21:841-854. DOI 10.1016/j.chembiol.2014.05.009 · PubMed

Other PDB entries of the same protein (UniProt O60885 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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