CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.20 | Single Sheet |
|
2.20.210 | ubp-family deubiquitinating enzyme fold |
|
2.20.210.10 | ubp-family deubiquitinating enzyme superfamily |
Domain Context
CATH Clusters
| Superfamily | ubp-family deubiquitinating enzyme superfamily |
| Functional Family |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q93009
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)
| Q93009 |
UBP7_HUMAN
Homo sapiens
Ubiquitin carboxyl-terminal hydrolase 7
|
PDB Structure
| PDB | 4M5X |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A 2.2 angstrom resolution structure of the USP7 catalytic domain in a new space group elaborates upon structural rearrangements resulting from ubiquitin binding.
Acta Crystallogr F Struct Biol Commun
|
