CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.130 | 7 Propeller | |
2.130.10 | Methylamine Dehydrogenase; Chain H | |
2.130.10.10 | YVTN repeat-like/Quinoprotein amine dehydrogenase |
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.
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UniProtKB Entries (2)
Q96RU8 |
TRIB1_HUMAN
Homo sapiens
Tribbles homolog 1
|
P43254 |
COP1_ARATH
Arabidopsis thaliana
E3 ubiquitin-protein ligase COP1
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PDB Structure
PDB | 5IGO |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural Basis for Substrate Selectivity of the E3 Ligase COP1.
Structure
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