2iph

X-ray diffraction
1.75Å resolution

X-ray Structure at 1.75 A Resolution of a Norovirus Protease Linked to an Active Site Directed Peptide 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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 19.31 KDa
Source organism: Southampton virus (serotype 3)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04544 (Residues: 1100-1280; 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: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 49.497Å b: 84.106Å c: 121.471Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.221
Expression system: Escherichia coli