CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.70 | Cathepsin B; Chain A |
|
3.90.70.10 | Cysteine proteinases |
Domain Context
CATH Clusters
| Superfamily | Cysteine proteinases |
| Functional Family | Ubiquitin carboxyl-terminal hydrolase 8 |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt P50102
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 (4)
| P84233 |
H32_XENLA
Xenopus laevis
Histone H3.2
|
| P0CG47 |
UBB_HUMAN
Homo sapiens
Polyubiquitin-B
|
| A6ZWK1 |
SGF11_YEAS7
Saccharomyces cerevisiae YJM789
SAGA-associated factor 11
|
| Q6WNK7 |
SUS1_YEAST
Saccharomyces cerevisiae S288C
Transcription and mRNA export factor SUS1
|
PDB Structure
| PDB | 4ZUX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for histone H2B deubiquitination by the SAGA DUB module.
Science
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