CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.930 | Outer Surface Protein A; domain 3 |
|
3.90.930.40 |
Domain Context
CATH Clusters
| Superfamily | 3.90.930.40 |
| Functional Family | ribosomal oxygenase 1 isoform X1 |
Enzyme Information
| 1.14.11.- |
With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors.
based on mapping to UniProt Q9H6W3
|
| 1.14.11.27 |
[Histone H3]-dimetyl-L-lysine-36 demethylase.
based on mapping to UniProt Q9H6W3
[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)
| Q9H6W3 |
RIOX1_HUMAN
Homo sapiens
Ribosomal oxygenase 1
|
PDB Structure
| PDB | 4CCK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Nature
|
