CATH Domain 4mdsA02

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	4MDS
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Discovery of N-(benzo[1,2,3]triazol-1-yl)-N-(benzyl)acetamido)phenyl) carboxamides as severe acute respiratory syndrome coronavirus (SARS-CoV) 3CLpro inhibitors: Identification of ML300 and noncovalent nanomolar inhibitors with an induced-fit binding. Turlington, M., Chun, A., Tomar, S., Eggler, A., Grum-Tokars, V., Jacobs, J., Daniels, J.S., Dawson, E., Saldanha, A., Chase, P., Baez-Santos, Y.M., Lindsley, C.W., Hodder, P., Mesecar, A.D., Stauffer, S.R. Bioorg.Med.Chem.Lett.