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4m9m

X-ray diffraction
1.53Å resolution

NS2B-NS3 protease from dengue virus at pH 8.5

Released:
Model geometry
Fit model/data
Source organism: dengue virus type 2
Primary publication:
Allosteric inhibition of the NS2B-NS3 protease from dengue virus.
ACS Chem Biol 8 2744-52 (2013)
PMID: 24164286

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-146327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease NS3 Chain: A
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 26.33 KDa
Source organism: dengue virus type 2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12823 (Residues: 1394-1440, 1476-1660; Coverage: 7%)
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X6A
Spacegroup: C2221
Unit cell:
a: 59.91Å b: 62.462Å c: 114.572Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.203 0.25
Expression system: Escherichia coli BL21(DE3)