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 NEDD4-like |
Enzyme Information
2.3.2.26 |
HECT-type E3 ubiquitin transferase.
based on mapping to UniProt P46934
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 (2)
P0CG53 |
UBB_BOVIN
Bos taurus
Polyubiquitin-B
|
P46934 |
NEDD4_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase NEDD4
|
PDB Structure
PDB | 4BBN |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structure of a Ubiquitin-Loaded Hect Ligase Reveals the Molecular Basis for Catalytic Priming
Nat.Struct.Mol.Biol.
|