P37296: V-type proton ATPase subunit a, Golgi isoform (STV1)

V-type proton ATPase subunit a, Golgi isoform (STV1) is a 890-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P37296.

Gene
STV1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
890 residues
Mean pLDDT
79.1
Model
AF-P37296-F1 v6
Model created
1 Aug 2025
PDB structures
4

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 79.1 (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 accurate32%
70 to 90Confident: backbone generally right47%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:11278748, PubMed:7514599). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:11278748, PubMed:7514599). Is present only in Golgi- and endosome-residing V-ATPase complexes; enzymes containing this subunit have a 4-fold lower ratio of proton transport to ATP hydrolysis than complexes containing the vacuolar isoform and do not dissociate V1 and V0 in response to glucose depletion (PubMed:11278748, PubMed:7514599)

Subunit structure

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1)

Subcellular location

Endosome membrane, Golgi apparatus membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6O7UEM3.1 Åa=1-890
6O7VEM6.6 Åa=1-890
6O7WEM7.0 Åa=1-890
6O7XEM8.7 Åa=1-890

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.