CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.10 | Thrombin, subunit H |
|
2.40.10.10 | Trypsin-like serine proteases |
Domain Context
CATH Clusters
| Superfamily | Trypsin-like serine proteases |
| Functional Family | Replicase polyprotein 1a |
Enzyme Information
| 3.4.22.69 |
SARS coronavirus main proteinase.
based on mapping to UniProt P0C6U8
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
-!- SARS coronavirus main protease is the key enzyme in SARS coronavirus replicase polyprotein processing. -!- Belongs to peptidase family C30.
|
| 3.4.22.- |
Cysteine endopeptidases.
based on mapping to UniProt P0C6U8
|
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt P0C6U8
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 (1)
| P0C6U8 |
R1A_CVHSA
Severe acute respiratory syndrome-related coronavirus
Replicase polyprotein 1a
|
PDB Structure
| PDB | 3IWM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Three-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main protease
Protein Cell
|
