CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.20 | Single Sheet | |
2.20.28 | Rubrerythrin, domain 2 | |
2.20.28.10 |
Domain Context
CATH Clusters
Superfamily | 2.20.28.10 |
Functional Family | RING finger and CHY zinc finger domain-containing protein 1 |
Enzyme Information
2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q96PM5
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.
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UniProtKB Entries (1)
Q96PM5 |
ZN363_HUMAN
Homo sapiens
RING finger and CHY zinc finger domain-containing protein 1
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PDB Structure
PDB | 2K2D |
External Links | |
Method | SOLUTION NMR |
Organism | Escherichia |
Primary Citation |
Molecular basis of Pirh2-mediated p53 ubiquitylation.
Nat.Struct.Mol.Biol.
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