CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.30 | Roll |
|
2.30.30 | SH3 type barrels. |
|
2.30.30.40 | SH3 Domains |
Domain Context
CATH Clusters
| Superfamily | SH3 Domains |
| Functional Family | E3 ubiquitin-protein ligase SH3RF1 |
Enzyme Information
| 2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q8BZT2
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.
-!- The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.
|
UniProtKB Entries (1)
| Q8BZT2 |
SH3R2_MOUSE
Mus musculus
Putative E3 ubiquitin-protein ligase SH3RF2
|
PDB Structure
| PDB | 2DJQ |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
The solution structure of the first SH3 domain of mouse SH3 domain containing ring finger 2
To be Published
|