2WP1: Brdt bromodomain 2

Structure of Brdt bromodomain 2 bound to an acetylated histone H3 peptide. Determined by X-ray diffraction at 2.1 Å resolution. Released 22 Sept 2009.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
MUS MUSCULUS
Chains
4
Atoms
2,247
Mol. weight
31.88 kDa
Released
22 Sept 2009

Explore 2WP1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WP1 contains 18 α-helices and 0 β-strands across 2 chains. 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-helix264-28219
α-helix285-2873
α-helix288-2914
α-helix292-2943
α-helix300-3034
α-helix308-3114
α-helix318-3269
α-helix333-35018
α-helix356-37217
Chain B: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix266-28217
α-helix285-2873
α-helix288-2914
α-helix292-2943
α-helix300-3034
α-helix308-3114
α-helix318-3269
α-helix333-35018
α-helix356-37318

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bromodomain testis-specific proteinA, Bprotein126MUS MUSCULUSQ91Y44 (AlphaFold model)
Histone H3P, Qprotein10MUS MUSCULUSP68433 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2WP1_1 BROMODOMAIN TESTIS-SPECIFIC PROTEIN (chains A, B)
QQQHKVLKTVKVTEQLKHCSEILKEMLAKKHLPYAWPFYNPVDADALGLHNYYDVVKNPM
DLGTIKGKMDNQEYKDAYEFAADVRLMFMNCYKYNPPDHEVVAMARTLQDVFELHFAKIP
DEPIES
Sequence of entity 2 (P, Q), FASTA
>2WP1_2 HISTONE H3 (chains P, Q)
KAPRKQLATK

Primary citation

Cooperative Binding of Two Acetylation Marks on a Histone Tail by a Single Bromodomain. Moriniere, J., Rousseaux, S., Steuerwald, U. et al. Nature (2009) 461:664. DOI 10.1038/NATURE08397 · PubMed

Other PDB entries of the same protein (UniProt Q91Y44 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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