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 | Recombination activating gene 1 |
Enzyme Information
| 2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt P15919
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.
|
| 3.1.-.- |
Acting on ester bonds.
based on mapping to UniProt P15919
|
UniProtKB Entries (1)
| P15919 |
RAG1_MOUSE
Mus musculus
V(D)J recombination-activating protein 1
|
PDB Structure
| PDB | 1RMD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster.
Nat.Struct.Biol.
|