×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily E3 ubiquitin-protein ligase SopA
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.
Lin, D.Y., Diao, J., Chen, J.
Proc.Natl.Acad.Sci.USA
CATH-Gene3D is a Global Biodata Core Resource Learn more...