CATH Domain 3v3mA02

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)

R1A_CVHSA

Severe acute respiratory syndrome-related coronavirus

Replicase polyprotein 1a

PDB Structure

PDB	3V3M
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Discovery, Synthesis, And Structure-Based Optimization of a Series of N-(tert-Butyl)-2-(N-arylamido)-2-(pyridin-3-yl) Acetamides (ML188) as Potent Noncovalent Small Molecule Inhibitors of the Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) 3CL Protease. Jacobs, J., Grum-Tokars, V., Zhou, Y., Turlington, M., Saldanha, S.A., Chase, P., Eggler, A., Dawson, E.S., Baez-Santos, Y.M., Tomar, S., Mielech, A.M., Baker, S.C., Lindsley, C.W., Hodder, P., Mesecar, A., Stauffer, S.R. J.Med.Chem.