4inh

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 dimer (preferred)
PDBe Complex ID:
PDB-CPX-164584 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
3C-like protease Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 185 amino acids
Theoretical weight: 19.64 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, syc59 Chains: J, M, N, O, P, Q, S, T
Molecule details ›
Chains: J, M, N, O, P, Q, S, T
Length: 4 amino acids
Theoretical weight: 497 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P1
Unit cell:
a: 56.335Å b: 66.917Å c: 100.459Å
α: 89.99° β: 90.09° γ: 75.93°
R-values:
R R work R free
0.178 0.176 0.208
Expression systems:
  • Escherichia coli
  • Not provided