P32842: V-type proton ATPase subunit c' (VMA11)

V-type proton ATPase subunit c' (VMA11) is a 164-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P32842.

Gene
VMA11
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
164 residues
Mean pLDDT
87.0
Model
AF-P32842-F1 v6
Model created
1 Aug 2025
PDB structures
28

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 87.0 (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 accurate58%
70 to 90Confident: backbone generally right32%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Proton-conducting pore forming 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:1837023, PubMed:9030535). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:1837023, PubMed:9030535)

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) (PubMed:27776355, PubMed:29526695). The decameric c-ring forms the proton-conducting pore, and is composed of eight proteolipid subunits c, one subunit c' and one subunit c'' (PubMed:27776355,…

Subcellular location

Vacuole membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8EASEM2.6 Åo=1-164
6M0REM2.7 ÅD=7-164
7TAPEM2.8 ÅD=1-164
6O7UEM3.1 Åo=1-164
6PE4EM3.1 ÅH=1-164
8EATEM3.1 Åo=1-164
8EAUEM3.1 Åo=1-164
6O7TEM3.2 Åo=1-164
6PE5EM3.2 ÅH=1-164
7TAOEM3.2 ÅD=1-164
9E7LEM3.33 ÅD=1-164
9E76EM3.4 ÅD=1-164
6C6LEM3.5 ÅD=1-164
7TMREM3.5 Åo=1-164
6M0SEM3.6 ÅD=7-164
9MJ4EM3.7 ÅD=1-164
7TMSEM3.8 Åo=1-164
7TMTEM3.8 Åo=1-164
5TJ5EM3.9 ÅD=17-163
7FDAEM4.2 ÅU=1-164

Showing 20 of 28 experimental structures (best resolution first).

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.