CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.58 | Methane Monooxygenase Hydroxylase; Chain G, domain 1 |
|
1.20.58.1360 |
Domain Context
CATH Clusters
| Superfamily | 1.20.58.1360 |
| Functional Family | Histone lysine demethylase PHF8 |
Enzyme Information
| 1.14.11.27 |
[Histone H3]-dimetyl-L-lysine-36 demethylase.
based on mapping to UniProt Q9UPP1
[Protein]-N(6),N(6)-dimethyl-L-lysine + 2 2-oxoglutarate + 2 O(2) = [protein]-L-lysine + 2 succinate + 2 formaldehyde + 2 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)
| Q9UPP1 |
PHF8_HUMAN
Homo sapiens
Histone lysine demethylase PHF8
|
PDB Structure
| PDB | 3KV4 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases.
Nat.Struct.Mol.Biol.
|