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:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assemblies composition:
Assembly name:
3C-like proteinase nsp5 and peptide (preferred)
PDBe Complex ID:
PDB-CPX-143065 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
3C-like proteinase nsp5
Molecule details ›
Chains: A, B, C, D
Length: 302 amino acids
Theoretical weight: 33.01 KDa
Source organism: Human coronavirus HKU1 (isolate N1)
Expression system: Escherichia coli
UniProt:
Sequence domains: Coronavirus endopeptidase C30
Structure domains:
Length: 302 amino acids
Theoretical weight: 33.01 KDa
Source organism: Human coronavirus HKU1 (isolate N1)
Expression system: Escherichia coli
UniProt:
- Canonical:
P0C6U3 (Residues: 3335-3634; Coverage: 7%)
Sequence domains: Coronavirus endopeptidase C30
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE BL-5A
Spacegroup:
P41
Expression systems:
- Escherichia coli
- Not provided
