Function and Biology Details
Reactions catalysed:
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
Sequence domains:
- P-loop containing nucleoside triphosphate hydrolase
- Helicase superfamily 1/2, ATP-binding domain
- Non-structural protein NS3, peptidase S7, flavivirus
- Helicase, C-terminal domain-like
- Non-structural protein NS3-like, DEAD box helicase, flavivirus
- Peptidase S1, PA clan
- Peptidase S1, PA clan, chymotrypsin-like fold
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174050 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DENGUE 4 NS3 FULL-LENGTH PROTEIN
Molecule details ›
Chain: A
Length: 618 amino acids
Theoretical weight: 69.52 KDa
Source organism: dengue virus type 4
Expression system: Escherichia coli BL21
UniProt:
Length: 618 amino acids
Theoretical weight: 69.52 KDa
Source organism: dengue virus type 4
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q2TN89 (Residues: 1475-2092; Coverage: 18%)
- Peptidase S7, Flavivirus NS3 serine protease
- Flavivirus DEAD domain
- Flavivirus NS3 helicase, C-terminal helical domain
Flavivirus NS2B domain-containing protein
Molecule details ›
Chain: B
Length: 31 amino acids
Theoretical weight: 2.9 KDa
Source organism: dengue virus type 4
Expression system: Escherichia coli BL21
UniProt:
Length: 31 amino acids
Theoretical weight: 2.9 KDa
Source organism: dengue virus type 4
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q91EQ2 (Residues: 101-123; Coverage: 17%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID23-1
Spacegroup:
P21
Expression system: Escherichia coli BL21
