Function and Biology Details
Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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.
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Viral protein genome-linked nsp9 (preferred)
PDBe Complex ID:
PDB-CPX-143101 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Papain-like protease nsp3
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.65 KDa
Source organism: Severe acute respiratory syndrome-related coronavirus
Expression system: Escherichia coli
UniProt:
Sequence domains: Betacoronavirus replicase NSP3, N-terminal
Structure domains: Ubiquitin-like (UB roll)
Length: 112 amino acids
Theoretical weight: 12.65 KDa
Source organism: Severe acute respiratory syndrome-related coronavirus
Expression system: Escherichia coli
UniProt:
- Canonical:
P0C6X7 (Residues: 819-930; Coverage: 2%)
Sequence domains: Betacoronavirus replicase NSP3, N-terminal
Structure domains: Ubiquitin-like (UB roll)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
94%
Refinement method:
torsion angle dynamics
Expression system: Escherichia coli
