Function and Biology Details
Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140544 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent RNA helicase vasa
Molecule details ›
Chains: B, D
Length: 163 amino acids
Theoretical weight: 18.25 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
Sequence domains: Helicase conserved C-terminal domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 163 amino acids
Theoretical weight: 18.25 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
- Canonical:
P09052 (Residues: 463-623; Coverage: 24%)
Sequence domains: Helicase conserved C-terminal domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Maternal effect protein oskar
Molecule details ›
Chains: A, C
Length: 107 amino acids
Theoretical weight: 11.92 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
Sequence domains: OST-HTH/LOTUS domain
Structure domains: LOTUS domain-like
Length: 107 amino acids
Theoretical weight: 11.92 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
- Canonical: P25158 (Residues: 139-240; Coverage: 17%)
Sequence domains: OST-HTH/LOTUS domain
Structure domains: LOTUS domain-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID23-1
Spacegroup:
P1
Expression system: Escherichia coli
