3l6p

X-ray diffraction
2.2Å resolution

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:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-148166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3; Serine protease subunit NS2B Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 25.06 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P33478 (Residues: 1393-1439, 1475-1499; Coverage: 2%)
  • Canonical: P17763 (Residues: 1501-1661; Coverage: 5%)
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: I222
Unit cell:
a: 56.721Å b: 60.848Å c: 161.644Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.239 0.284
Expression system: Escherichia coli BL21(DE3)