2DWW: Bromodomain-containing protein 4

Crystal structure of Bromodomain-containing protein 4. Determined by X-ray diffraction at 1.8 Å resolution. Released 21 Aug 2007.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Mus musculus
Chains: 1
Atoms: 1,113
Mol. weight: 13.71 kDa
Released: 21 Aug 2007

Explore 2DWW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2DWW contains 8 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: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	3-19	17
α-helix	22-24	3
α-helix	25-28	4
α-helix	29-31	3
α-helix	45-48	4
α-helix	55-63	9
α-helix	70-87	18
α-helix	93-111	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bromodomain-containing protein 4	A	protein	114	Mus musculus	Q9ESU6 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2DWW_1 Bromodomain-containing protein 4 (chains A)
KSSKISEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKS
KLESREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPD

Primary citation

Crystal structure of Bromodomain-containing protein 4. Padmanabhan, B., Yokoyama, S. To be published.

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

3JVL 1.2 Å, Crystal structure of bromodomain 2 of mouse Brd4
3JVM 1.2 Å, Crystal structure of bromodomain 2 of mouse Brd4
3JVJ 1.55 Å, Crystal structure of the bromodomain 1 in mouse Brd4
3MUL 1.65 Å, Crystal structure of Brd4 bromodomain 1 with butyrylated histone H3-K(buty)14
3MUK 1.75 Å, Crystal structure of Brd4 bromodomain 1 with propionylated histone H3-K(prop)23
3JVK 1.8 Å, Crystal structure of bromodomain 1 of mouse Brd4 in complex with histone H3-K(ac)14
2JNS Solution structure of the Bromodomain-containing protein 4 ET domain

Browse structure collections

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