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.
Explore 2O94 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 64-124 | 61 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 64-124 | 61 | |
| α-helix | 126-128 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone deacetylase 4 | A, B, C, D | protein | 112 | Homo sapiens | P56524 (AlphaFold model) |
>2O94_1 Histone deacetylase 4 (chains A, B, C, D) GSSHHHHHHSSGLVPRGSHMAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQFEQLS RQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQ
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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