CATH Classification

Domain Context

CATH Clusters

Superfamily Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Functional Family Proteasome subunit beta type-2

Enzyme Information

3.4.25.1
Proteasome endopeptidase complex.
based on mapping to UniProt P25043
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)

P30656
PSB5_YEAST
Saccharomyces cerevisiae S288C
Proteasome subunit beta type-5

PDB Structure

PDB 4LTC
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Enzyme inhibition by hydroamination: design and mechanism of a hybrid carmaphycin-syringolin enone proteasome inhibitor.
Trivella, D.B., Pereira, A.R., Stein, M.L., Kasai, Y., Byrum, T., Valeriote, F.A., Tantillo, D.J., Groll, M., Gerwick, W.H., Moore, B.S.
Chem.Biol.