CATH Classification

Domain Context

CATH Clusters

Superfamily YVTN repeat-like/Quinoprotein amine dehydrogenase
Functional Family E3 ubiquitin-protein ligase RFWD2 isoform X1

Enzyme Information

2.3.2.27
RING-type E3 ubiquitin transferase.
based on mapping to UniProt P43254
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.
-!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an 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 and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31.

UniProtKB Entries (2)

Q96RU8
TRIB1_HUMAN
Homo sapiens
Tribbles homolog 1
P43254
COP1_ARATH
Arabidopsis thaliana
E3 ubiquitin-protein ligase COP1

PDB Structure

PDB 5IGO
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Basis for Substrate Selectivity of the E3 Ligase COP1.
Uljon, S., Xu, X., Durzynska, I., Stein, S., Adelmant, G., Marto, J.A., Pear, W.S., Blacklow, S.C.
Structure