CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.20 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
|
3.60.20.10 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
| Functional Family | Proteasome subunit alpha |
Enzyme Information
| 3.4.25.1 |
Proteasome endopeptidase complex.
based on mapping to UniProt Q53080
Cleavage of peptide bonds with very broad specificity.
-!- A 20-S protein composed of 28 subunits arranged in four rings of seven. -!- The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity. -!- In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. -!- The molecule is barrel-shaped, and the active sites are on the inner surfaces. -!- Terminal apertures restrict access of substrates to the active sites. -!- Inhibited by mercurial reagents and some inhibitors of serine endopeptidases. -!- Belongs to peptidase family T1. -!- Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
|
UniProtKB Entries (1)
| Q53079 |
PSB1_RHOER
Rhodococcus erythropolis
Proteasome subunit beta 1
|
PDB Structure
| PDB | 1Q5Q |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structures of the Rhodococcus proteasome with and without its pro-peptides: implications for the role of the pro-peptide in proteasome assembly.
J.Mol.Biol.
|