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 1Q2W
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
X-Ray Crystal Structure of the SARS Coronavirus Main Protease
Bonanno, J.B., Fowler, R., Gupta, S., Hendle, J., Lorimer, D., Romero, R., Sauder, J.M., Wei, C.L., Liu, E.T., Burley, S.K., Harris, T.
To be Published