3MUK: Bromodomain-containing protein 4

Crystal structure of Brd4 bromodomain 1 with propionylated histone H3-K(prop)23. Determined by X-ray diffraction at 1.75 Å resolution. Released 11 Aug 2010.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Mus musculus
Chains
2
Atoms
1,230
Mol. weight
16.34 kDa
Released
11 Aug 2010

Explore 3MUK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3MUK contains 9 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: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix44-496
α-helix61-655
α-helix66-716
α-helix72-754
α-helix81-833
α-helix97-1004
α-helix107-1159
α-helix122-13918
α-helix145-16117

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bromodomain-containing protein 4Aprotein131Mus musculusQ9ESU6 (AlphaFold model)
peptide of Histone H3.3Dprotein8P84243 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3MUK_1 Bromodomain-containing protein 4 (chains A)
GAMGSTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDY
YKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLF
LQKINELPTEE
Sequence of entity 2 (D), FASTA
>3MUK_2 peptide of Histone H3.3 (chains D)
ATXAARKS

Primary citation

Interaction of propionylated and butyrylated histone H3 lysine marks with Brd4 bromodomains. Vollmuth, F., Geyer, M. Angew Chem Int Ed Engl (2010) 49:6768-6772. DOI 10.1002/anie.201002724 · PubMed

Other PDB entries of the same protein (UniProt Q9ESU6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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