2ihs

X-ray diffraction
2.2Å resolution

Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide

Released:
Source organism: Drosophila melanogaster
Primary publication:
Structural basis for protein recognition by B30.2/SPRY domains.
Mol. Cell 24 967-76 (2006)
PMID: 17189197

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 dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein gustavus Chains: A, B
Molecule details ›
Chains: A, B
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%)
Gene names: CG2944, gus
Sequence domains: SPRY domain
ATP-dependent RNA helicase vasa Chains: C, D
Molecule details ›
Chains: C, D
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%)
Gene names: CG46283, vas, vasa

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P41212
Unit cell:
a: 80.209Å b: 80.209Å c: 159.798Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.26
Expression system: Escherichia coli