6bib

X-ray diffraction
1.95Å resolution

1.95 A resolution structure of Norovirus 3CL protease in complex with a triazole-based macrocyclic inhibitor

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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 188 amino acids
Theoretical weight: 20.13 KDa
Source organism: Norovirus Hu/1968/US
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q83883 (Residues: 1101-1281; Coverage: 10%)
Gene name: ORF1
Sequence domains: Southampton virus-type processing peptidase
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 17-ID
Spacegroup: P212121
Unit cell:
a: 37.873Å b: 67.191Å c: 126.576Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.24
Expression system: Escherichia coli BL21