CATH Classification

Domain Context

CATH Clusters

Superfamily YVTN repeat-like/Quinoprotein amine dehydrogenase
Functional Family E3 ubiquitin-protein ligase COP1

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.
-!- The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the 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 an the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.

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