CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 2 | Mainly Beta | 
|   | 2.60 | Sandwich | 
|   | 2.60.40 | Immunoglobulin-like | 
|   | 2.60.40.150 | C2 domain | 
Domain Context
CATH Clusters
| Superfamily | C2 domain | 
| Functional Family | E3 ubiquitin-protein ligase | 
Enzyme Information
| 2.3.2.26 | HECT-type E3 ubiquitin transferase. based on mapping to UniProt Q9HCE7 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)
| Q9HCE7 | SMUF1_HUMAN Homo sapiens E3 ubiquitin-protein ligase SMURF1 | 
PDB Structure
| PDB | 3PYC | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Crystal structure of human SMURF1 C2 domain To be Published | 
