CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.160 | Double Stranded RNA Binding Domain |
|
3.30.160.60 | Classic Zinc Finger |
Domain Context
CATH Clusters
| Superfamily | Classic Zinc Finger |
| Functional Family | Tripartite motif-containing 5 (Predicted) |
Enzyme Information
| 2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt P19474
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.
-!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an 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 and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31.
|
UniProtKB Entries (1)
| P19474 |
RO52_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase TRIM21
|
PDB Structure
| PDB | 5JPX |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
Solution NMR structure of the TRIM21 B-box2 and identification of residues involved in its interaction with the RING domain.
PLoS ONE
|
