CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.4140 | effector protein (NleL) fold |
|
1.10.4140.10 | effector protein (NleL) |
Domain Context
CATH Clusters
| Superfamily | effector protein (NleL) |
| Functional Family | SPI-1 type III secretion system effector HECT-type E3 ubiquitin transferase SopA |
Enzyme Information
| 2.3.2.26 |
HECT-type E3 ubiquitin transferase.
based on mapping to UniProt Q8ZNR3
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)
| P68036 |
UB2L3_HUMAN
Homo sapiens
Ubiquitin-conjugating enzyme E2 L3
|
| Q8ZNR3 |
SOPA_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
E3 ubiquitin-protein ligase SopA
|
PDB Structure
| PDB | 3SY2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions.
Proc.Natl.Acad.Sci.USA
|
