Function and Biology Details
Reactions catalysed:
GTP + a 5'-diphospho-[mRNA] = diphosphate + a 5'-(5'-triphosphoguanosine)-[mRNA]
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).
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.
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
3C-like proteinase nsp5 (preferred)
PDBe Complex ID:
PDB-CPX-143071 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Papain-like protease nsp3
Molecule details ›
Chain: A
Length: 67 amino acids
Theoretical weight: 7.6 KDa
Source organism: Severe acute respiratory syndrome-related coronavirus
Expression system: Escherichia coli
UniProt:
Sequence domains: Betacoronavirus SUD-C domain
Structure domains: Coronavirus polyprotein cleavage domain
Length: 67 amino acids
Theoretical weight: 7.6 KDa
Source organism: Severe acute respiratory syndrome-related coronavirus
Expression system: Escherichia coli
UniProt:
- Canonical:
P0C6U8 (Residues: 1473-1538; Coverage: 2%)
Sequence domains: Betacoronavirus SUD-C domain
Structure domains: Coronavirus polyprotein cleavage domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
torsion angle dynamics, energy minimization
Expression system: Escherichia coli
