4in1

X-ray diffraction
2.05Å resolution

Structural Basis of Substrate Specificity and Protease Inhibition in Norwalk Virus

Released:

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182857 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like protease Chain: A
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 19.34 KDa
Source organism: Norovirus Hu/1968/US
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83883 (Residues: 1101-1281; Coverage: 10%)
Gene name: ORF1
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6522
Unit cell:
a: 124.197Å b: 124.197Å c: 49.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.163 0.201
Expression system: Escherichia coli