CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.80 | Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 |
Domain Context
CATH Clusters
| Superfamily | Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 |
| Functional Family | ubiquitin-like modifier-activating enzyme 1 |
Enzyme Information
| 6.2.1.45 |
E1 ubiquitin-activating enzyme.
based on mapping to UniProt P22314
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.
-!- Catalyzes the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. -!- The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.
|
UniProtKB Entries (1)
| P62979 |
RS27A_HUMAN
Homo sapiens
Ubiquitin-40S ribosomal protein S27a
|
PDB Structure
| PDB | 6DC6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of a human ubiquitin E1-ubiquitin complex reveals conserved functional elements essential for activity.
J. Biol. Chem.
|
