CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.20 | Single Sheet |
|
2.20.70 | Ubiquitin Ligase Nedd4; Chain: W; |
|
2.20.70.10 |
Domain Context
CATH Clusters
| Superfamily | 2.20.70.10 |
| Functional Family | E3 ubiquitin-protein ligase |
Enzyme Information
| 2.3.2.26 |
HECT-type E3 ubiquitin transferase.
based on mapping to UniProt Q9HAU4
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. -!- In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon- amino group of an L-lysine residue of the acceptor protein. -!- Cf. EC 2.3.2.27 and EC 2.3.2.31.
|
UniProtKB Entries (1)
| O15105 |
SMAD7_HUMAN
Homo sapiens
Mothers against decapentaplegic homolog 7
|
PDB Structure
| PDB | 2DJY |
| External Links | |
| Method | SOLUTION NMR |
| Organism | Escherichia |
| Primary Citation |
An Expanded WW Domain Recognition Motif Revealed by the Interaction between Smad7 and the E3 Ubiquitin Ligase Smurf2.
J.Biol.Chem.
|
