5y6n

X-ray diffraction
1.57Å resolution

Zika virus helicase in complex with ADP

Released:
Source organism: Zika virus
Primary publication:
Mechanism of ATP hydrolysis by the Zika virus helicase.
FASEB J 32 5250-5257 (2018)
PMID: 29913559

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-100062 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3 Chain: A
Molecule details ›
Chain: A
Length: 438 amino acids
Theoretical weight: 49.34 KDa
Source organism: Zika virus
Expression system: Escherichia coli 536
UniProt:
  • Canonical: A0A024B7W1 (Residues: 1682-2119; Coverage: 13%)
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P21
Unit cell:
a: 63.275Å b: 52.934Å c: 64.483Å
α: 90° β: 104.93° γ: 90°
R-values:
R R work R free
0.182 0.182 0.202
Expression system: Escherichia coli 536