5rhg

X-ray diffraction
1.41Å resolution

PanDDA analysis group deposition -- Crystal Structure of Zika virus NS3 Helicase in complex with Z235341991

Released:
Model geometry
Fit model/data
Source organism: Zika virus
Entry authors: Godoy AS, Mesquita NCMR, Oliva G

Function and Biology Details

Reactions catalysed:
a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine.
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA +S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H(+).
RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaacan be either Arg or Lys and Yaa can be either Ser or Ala.
a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate+ phosphate + H(+).
ATP + H2O = ADP + phosphate + H(+).
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-174291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3 Chain: A
Molecule details ›
Chain: A
Length: 435 amino acids
Theoretical weight: 48.95 KDa
Source organism: Zika virus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q32ZE1 (Residues: 1681-2115; Coverage: 13%)
Sequence domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 53.777Å b: 68.692Å c: 57.183Å
α: 90° β: 92.61° γ: 90°
R-values:
R R work R free
0.176 0.174 0.205
Expression system: Escherichia coli