CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
6 | Special |
|
6.10 | Helix non-globular |
|
6.10.250 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
6.10.250.1550 |
Domain Context
CATH Clusters
| Superfamily | 6.10.250.1550 |
| Functional Family |
Enzyme Information
| 3.5.1.98 |
Histone deacetylase.
based on mapping to UniProt P56524
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
-!- A class of enzymes that remove acetyl groups from N(6)-acetyl-lysine residues on a histone. -!- The reaction of this enzyme is opposite to that of EC 2.3.1.48. -!- Histone deacetylases (HDACs) can be organized into three classes depending on sequence similarity and domain organization. -!- Histone acetylation plays an important role in regulation of gene expression. -!- In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation. -!- May be identical to EC 3.5.1.17.
|
UniProtKB Entries (1)
| P56524 |
HDAC4_HUMAN
Homo sapiens
Histone deacetylase 4
|
PDB Structure
| PDB | 2O94 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains.
Proc.Natl.Acad.Sci.Usa
|
