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 beta type-1 |
Enzyme Information
3.4.25.1 |
Proteasome endopeptidase complex.
based on mapping to UniProt P38624
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 (2)
P40306 |
PSB10_HUMAN
Homo sapiens
Proteasome subunit beta type-10
|
P32379 |
PSA5_YEAST
Saccharomyces cerevisiae S288C
Proteasome subunit alpha type-5
|
PDB Structure
PDB | 6HV4 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structure-Based Design of Inhibitors Selective for Human Proteasome beta 2c or beta 2i Subunits.
J.Med.Chem.
|