X-ray diffraction
2.35Å resolution

Crystal structure of the glycoprotein Erns from the pestivirus BVDV-1 in complex with 5'-CMP

Entry authors: Krey T, Bontems F, Vonrhein C, Vaney M-C, Bricogne G, Ruemenapf T, Rey FA

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
NTP + H(2)O = NDP + phosphate
Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites
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
Macromolecules (3 distinct):
E(rns) glycoprotein Chains: A, B
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 19.01 KDa
Source organism: Bovine viral diarrhea virus 1-CP7
Expression system: Drosophila melanogaster
  • Canonical: Q96662 (Residues: 271-435; Coverage: 4%)
Structure domains: Ribonuclease T2-like

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 70.93Å b: 106.46Å c: 64.03Å
α: 90° β: 90° γ: 90°
R R work R free
0.188 0.186 0.221
Expression system: Drosophila melanogaster