CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.800 | Arginase; Chain A |
|
3.40.800.20 | Histone deacetylase domain |
Domain Context
CATH Clusters
| Superfamily | Histone deacetylase domain |
| Functional Family | Histone deacetylase |
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 | 2VQM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and Functional Analysis of the Human Hdac4 Catalytic Domain Reveals a Regulatory Zinc-Binding Domain.
J.Biol.Chem.
|