CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.40 | Herpes Virus-1 |
|
3.30.40.10 | Zinc/RING finger domain, C3HC4 (zinc finger) |
Domain Context
CATH Clusters
| Superfamily | Zinc/RING finger domain, C3HC4 (zinc finger) |
| Functional Family | Histone lysine demethylase PHF8 |
Enzyme Information
| 1.14.11.27 |
[Histone H3]-lysine-36 demethylase.
based on mapping to UniProt Q80TJ7
(1) Protein N(6),N(6)-dimethyl-L-lysine + 2-oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO(2). (2) Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O(2) = protein L-lysine + succinate + formaldehyde + CO(2).
-!- Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys-36. -!- Lysine residues exist in three methylation states (mono-, di- and trimethylated). -!- The enzyme preferentially demethylates the dimethyl form of Lys-36 (K36me2), which is its natural substrate, to form the monomethyl and unmethylated forms of Lys-36. -!- It can also demethylate the monomethyl- but not the trimethyl form of Lys-36.
|
UniProtKB Entries (1)
| Q80TJ7 |
PHF8_MOUSE
Mus musculus
Histone lysine demethylase PHF8
|
PDB Structure
| PDB | 1WEP |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
Solution structure of PHD domain in protein AA017385
To be Published
|
