3LXJ: Bromodomain of Human AAA domain containing 2B

Crystal Structure of the Bromodomain of Human AAA domain containing 2B (ATAD2B). Determined by X-ray diffraction at 2.33 Å resolution. Released 9 Mar 2010.

Method
X-ray diffraction
Resolution
2.33 Å
Organism
Homo sapiens
Chains
4
Atoms
4,424
Mol. weight
63.64 kDa
Ligands
IPA
Released
9 Mar 2010

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

Secondary structure: helices and β-sheets

3LXJ contains 32 α-helices and 0 β-strands across 4 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-helix952-97524
α-helix978-9803
α-helix986-9883
α-helix995-9984
α-helix1005-10139
α-helix1020-103718
α-helix1043-106624
α-helix1069-108315
Chain B: 7 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix952-97524
α-helix978-9836
α-helix995-9984
α-helix1005-10139
α-helix1020-103718
α-helix1043-106624
α-helix1069-108416
Chain C: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix953-97523
α-helix978-9836
α-helix986-9883
α-helix990-9923
α-helix995-9973
α-helix1005-10139
α-helix1020-103718
α-helix1043-106624
α-helix1069-108315
Chain D: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix955-97521
α-helix978-9836
α-helix986-9883
α-helix992-9987
α-helix1005-10139
α-helix1020-103718
α-helix1043-106624
α-helix1069-108315

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ATPase family AAA domain-containing protein 2BA, B, C, Dprotein136Homo sapiensQ9ULI0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>3LXJ_1 ATPase family AAA domain-containing protein 2B (chains A, B, C, D)
SMEDQEENTLRELRLFLRDVTKRLATDKRFNIFSKPVDIEEVSDYLEVIKEPMDLSTVIT
KIDKHNYLTAKDFLKDIDLICSNALEYNPDKDPGDKIIRHRACTLKDTAHAIIAAELDPE
FNKLCEEIKEARIKRG

Ligands and cofactors

IDNameFormulaCopies
IPAIsopropyl alcoholC3 H8 O5

Primary citation

Histone recognition and large-scale structural analysis of the human bromodomain family. Filippakopoulos, P., Picaud, S., Mangos, M. et al. Cell (2012) 149:214-231. DOI 10.1016/j.cell.2012.02.013 · PubMed

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

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