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).
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Non-structural protein 4 and peptide (preferred)
PDBe Complex ID:
PDB-CPX-143132 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
3C-like proteinase nsp5
Molecule details ›
Chains: A, B, C
Length: 301 amino acids
Theoretical weight: 33.06 KDa
Source organism: Murine hepatitis virus strain A59
Expression system: Escherichia coli
UniProt:
Sequence domains: Coronavirus endopeptidase C30
Structure domains:
Length: 301 amino acids
Theoretical weight: 33.06 KDa
Source organism: Murine hepatitis virus strain A59
Expression system: Escherichia coli
UniProt:
- Canonical:
P0C6X9 (Residues: 3334-3620, 3621-3635; Coverage: 4%)
Sequence domains: Coronavirus endopeptidase C30
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRF BEAMLINE BL17B1
Spacegroup:
C2
Expression systems:
- Escherichia coli
- Not provided
