CATH Classification

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 3F9H
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure.
Hu, T., Zhang, Y., Li, L., Wang, K., Chen, S., Chen, J., Ding, J., Jiang, H., Shen, X.
Virology