2O94: Histone deacetylase 4

The 97H/F mutant Structure of a glutamine-rich domain from histone deacetylase 4. Determined by X-ray diffraction at 3.0 Å resolution. Released 27 Feb 2007.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Homo sapiens
Chains
4
Atoms
2,328
Mol. weight
54.65 kDa
Released
27 Feb 2007

Explore 2O94 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2O94 contains 5 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.

Chains A, B and C: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix64-12461
Chain D: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix64-12461
α-helix126-1283

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone deacetylase 4A, B, C, Dprotein112Homo sapiensP56524 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2O94_1 Histone deacetylase 4 (chains A, B, C, D)
GSSHHHHHHSSGLVPRGSHMAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQFEQLS
RQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQ

Primary citation

Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Guo, L., Han, A., Bates, D.L. et al. Proc Natl Acad Sci U S A (2007) 104:4297-4302. DOI 10.1073/pnas.0608041104 · PubMed

Other PDB entries of the same protein (UniProt P56524 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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