CATH Classification

Domain Context

CATH Clusters

Superfamily Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Functional Family

Enzyme Information

3.4.25.1
Proteasome endopeptidase complex.
based on mapping to UniProt A5U4D5
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)

A5U4D5
PSA_MYCTA
Mycobacterium tuberculosis H37Ra
Proteasome subunit alpha

PDB Structure

PDB 5THO
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Basis for the Species-Selective Binding of N,C-Capped Dipeptides to the Mycobacterium tuberculosis Proteasome.
Hsu, H.C., Singh, P.K., Fan, H., Wang, R., Sukenick, G., Nathan, C., Lin, G., Li, H.
Biochemistry
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