Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|- and the P1' position is occupied by Gly-|-
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Viral genome-linked protein (preferred)
PDBe Complex ID:
PDB-CPX-182353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like protease
Molecule details ›
Chains: A, B
Length: 179 amino acids
Theoretical weight: 18.82 KDa
Source organism: Murine norovirus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Southampton virus-type processing peptidase
Structure domains: Trypsin-like serine proteases
Length: 179 amino acids
Theoretical weight: 18.82 KDa
Source organism: Murine norovirus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q80J95 (Residues: 998-1173; Coverage: 10%)
Sequence domains: Southampton virus-type processing peptidase
Structure domains: Trypsin-like serine proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-007 HF
Spacegroup:
P1
Expression system: Escherichia coli BL21(DE3)
