P09052: ATP-dependent RNA helicase vasa (vas)

ATP-dependent RNA helicase vasa (vas) is a 661-residue protein from Drosophila melanogaster. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P09052.

Gene
vas
Organism
Drosophila melanogaster
Length
661 residues
Mean pLDDT
72.3
Model
AF-P09052-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate48%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions34%

What pLDDT means and how to read it

Function

Involved in translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or structural integrity of perinuclear nuage particles during germ cell formation. Required for gus, Fsn and aub accumulation at the posterior pole of the embryo. Required for the localization of vas to the perinuclear region of nurse cells. May have a role in production of piwi-interacting RNA (piRNA) (PubMed:17428915)

Subunit structure

Interacts with eIF5B and faf. Interacts with gus (via B30.2/SPRY domain) and Fsn (via B30.2/SPRY domain). Interacts with aub, me31B, eIF-4a and TER94. Interacts with piwi; this interaction is RNA independent. Interacts with Dcr-1 and Fmr1; these interactions occur in the polar granules

Subcellular location

Cytoplasm, Cytoplasm, perinuclear region, Cytoplasm, Cytoplasmic ribonucleoprotein granule

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5NT7X-ray1.4 ÅB/D=463-623
3EMWX-ray1.8 ÅB=184-203
3F2OX-ray2.05 ÅC/D=184-203
2DB3X-ray2.2 ÅA/B/C/D=200-623
2IHSX-ray2.2 ÅC/D=184-203

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