Function and Biology Details
Reactions catalysed:
ATP + RNA(n) = diphosphate + RNA(n+1)
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
ADP-D-ribose 1''-phosphate + H(2)O = ADP-D-ribose + phosphate
NTP + H(2)O = NDP + phosphate
A 5'-triphospho-[mRNA] + H(2)O = a 5'-diphospho-[mRNA] + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Non-structural protein 3 (preferred)
PDBe Complex ID:
PDB-CPX-153170 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Non-structural protein 3
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 18.36 KDa
Source organism: Venezuelan equine encephalitis virus (strain P676)
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Leucine Aminopeptidase, subunit E, domain 1
Length: 168 amino acids
Theoretical weight: 18.36 KDa
Source organism: Venezuelan equine encephalitis virus (strain P676)
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P36328 (Residues: 1330-1489; Coverage: 6%)
Structure domains: Leucine Aminopeptidase, subunit E, domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
83%
Refinement method:
molecular dynamics
Expression system: Escherichia coli BL21(DE3)
