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.
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UniProtKB Entries (1)
P0C6U8 |
R1A_CVHSA
Severe acute respiratory syndrome-related coronavirus
Replicase polyprotein 1a
|
PDB Structure
PDB | 3IWM |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Three-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main protease
Protein Cell
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