Function and Biology Details
Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106771 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein gustavus
Molecule details ›
Chains: A, B
Length: 214 amino acids
Theoretical weight: 24.18 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
Sequence domains: SPRY domain
Length: 214 amino acids
Theoretical weight: 24.18 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
- Canonical:
A1Z6E0 (Residues: 27-232; Coverage: 74%)
Sequence domains: SPRY domain
ATP-dependent RNA helicase vasa
Molecule details ›
Chains: C, D
Length: 20 amino acids
Theoretical weight: 2.5 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
Length: 20 amino acids
Theoretical weight: 2.5 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
- Canonical: P09052 (Residues: 184-203; Coverage: 3%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup:
P41212
Expression system: Escherichia coli
