CATH Classification

Domain Context

CATH Clusters

Superfamily Ubiquitin Conjugating Enzyme
Functional Family Ubiquitin-conjugating enzyme E2 L3

Enzyme Information

2.3.2.23
E2 ubiquitin-conjugating enzyme.
based on mapping to UniProt P68036
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine.
-!- The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. -!- In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage. -!- Formerly EC 6.3.2.19.

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
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