8SDX: ATAD2B bromodomain

ATAD2B bromodomain in complex with histone H4 acetylated at lysine 5 with Serine 1 mutation to Cysteine. Determined by X-ray diffraction at 2.69 Å resolution. Released 5 Jun 2024.

Method
X-ray diffraction
Resolution
2.69 Å
Organism
Homo sapiens
Chains
4
Atoms
2,342
Mol. weight
34.44 kDa
Released
5 Jun 2024

Explore 8SDX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SDX contains 16 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: 8 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix952-97625
α-helix979-9835
α-helix986-9883
α-helix995-9984
α-helix1005-10139
α-helix1020-103718
α-helix1043-106624
α-helix1069-108214
Chain B: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix954-97522
α-helix979-9835
α-helix986-9872
α-helix995-9984
α-helix1005-10139
α-helix1020-103718
α-helix1043-106624
α-helix1069-108214

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ATPase family AAA domain-containing protein 2BA, Bprotein136Homo sapiensQ9ULI0 (AlphaFold model)
histone H4S1CK5acC, Dprotein15Homo sapiensP62805 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>8SDX_1 ATPase family AAA domain-containing protein 2B (chains A, B)
GPLEDQEENTLRELRLFLRDVTKRLATDKRFNIFSKPVDIEEVSDYLEVIKEPMDLSTVI
TKIDKHNYLTAKDFLKDIDLICSNALEYNPDKDPGDKIIRHRACTLKDTAHAIIAAELDP
EFNKLCEEIKEARIKR
Sequence of entity 2 (C, D), FASTA
>8SDX_2 histone H4S1CK5ac (chains C, D)
CGRGKGGKGLGKGGA

Primary citation

Impact of Combinatorial Histone Modifications on Acetyllysine Recognition by the ATAD2 and ATAD2B Bromodomains. Phillips, M., Malone, K.L., Boyle, B.W. et al. J Med Chem (2024) 67:8186-8200. DOI 10.1021/acs.jmedchem.4c00210 · PubMed

Other PDB entries of the same protein (UniProt Q9ULI0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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