4imz

X-ray diffraction
1.7Å 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:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-164583 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
3C-like protease Chain: A
Molecule details ›
Chain: A
Length: 183 amino acids
Theoretical weight: 19.41 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
peptide inhibitor, syc 10 Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 573 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6522
Unit cell:
a: 122.575Å b: 122.575Å c: 51.126Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.163 0.194
Expression systems:
  • Escherichia coli
  • Not provided