CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1750 | Hect, E3 ligase catalytic domain fold |
|
3.90.1750.10 | Hect, E3 ligase catalytic domains |
Domain Context
CATH Clusters
| Superfamily | Hect, E3 ligase catalytic domains |
| Functional Family | E3 ubiquitin-protein ligase |
Enzyme Information
| 2.3.2.26 |
HECT-type E3 ubiquitin transferase.
based on mapping to UniProt Q9H0M0
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)
| Q9H0M0 |
WWP1_HUMAN
Homo sapiens
NEDD4-like E3 ubiquitin-protein ligase WWP1
|
PDB Structure
| PDB | 1ND7 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase
Mol.Cell
|
