CATH Domain 3vb5A03

CATH Classification

Level	CATH Code	Description
	1	Mainly Alpha
	1.10	Orthogonal Bundle
	1.10.1840	main proteinase (3clpro) structure, domain 3
	1.10.1840.10	main proteinase (3clpro) structure, domain 3

Domain Context

CATH Clusters

Superfamily	main proteinase (3clpro) structure, domain 3
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	3VB5
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Design, synthesis and crystallographic analysis of nitrile-based broad-spectrum peptidomimetic inhibitors for coronavirus 3C-like proteases Chuck, C.P., Chen, C., Ke, Z., Wan, D.C.-C., Chow, H.F., Wong, K.B. Eur.J.Med.Chem.