CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.110 | Ubiquitin Conjugating Enzyme |
|
3.10.110.10 | Ubiquitin Conjugating Enzyme |
Domain Context
CATH Clusters
| Superfamily | Ubiquitin Conjugating Enzyme |
| Functional Family | ubiquitin-conjugating enzyme E2 27 |
Enzyme Information
| 2.3.2.23 |
E2 ubiquitin-conjugating enzyme.
based on mapping to UniProt P21734
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)
| P21734 |
UBC1_YEAST
Saccharomyces cerevisiae S288C
Ubiquitin-conjugating enzyme E2 1
|
| P0CG48 |
UBC_HUMAN
Homo sapiens
Polyubiquitin-C
|
PDB Structure
| PDB | 1FXT |
| External Links | |
| Method | SOLUTION NMR |
| Organism | Escherichia |
| Primary Citation |
Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail.
Structure
|
