CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
6 | Special |
|
6.10 | Helix non-globular |
|
6.10.250 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
6.10.250.1720 |
Domain Context
CATH Clusters
| Superfamily | 6.10.250.1720 |
| Functional Family |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q96RU2
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
-!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12.
|
UniProtKB Entries (1)
| Q96RU2 |
UBP28_HUMAN
Homo sapiens
Ubiquitin carboxyl-terminal hydrolase 28
|
PDB Structure
| PDB | 2LVA |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
NMR solution structure of the N-terminal domain of human USP28
To be Published
|