6w5l

X-ray diffraction
2.1Å resolution

2.1 A resolution structure of Norovirus 3CL protease in complex with inhibitor 7g

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, C, D
Molecule details ›
Chains: A, B, C, D
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

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P1
Unit cell:
a: 37.435Å b: 37.859Å c: 115.535Å
α: 91.65° β: 96.44° γ: 95.44°
R-values:
R R work R free
0.207 0.204 0.267
Expression system: Escherichia coli BL21