P31412: V-type proton ATPase subunit C (VMA5)

V-type proton ATPase subunit C (VMA5) is a 392-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P31412.

Gene
VMA5
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
392 residues
Mean pLDDT
89.5
Model
AF-P31412-F1 v6
Model created
1 Aug 2025
PDB structures
18

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.5 (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 accurate72%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Subunit of the V1 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:10781598, PubMed:11777935, PubMed:1730668, PubMed:8416931). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:8416931). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (PubMed:15792803). Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section (PubMed:15792803)

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:25971514). Interacts directly with VMA4 (PubMed:15751969)

Subcellular location

Vacuole membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1U7LX-ray1.75 ÅA=1-392
4EFAX-ray2.82 ÅC=158-277
4DL0X-ray2.9 ÅC/I=158-277
7TMMEM3.5 ÅO=1-392
7TMREM3.5 ÅO=1-392
7FDEEM3.8 ÅO=1-392
7FDAEM4.2 ÅO=1-392
7FDBEM4.8 ÅO=1-392
6O7VEM6.6 ÅO=1-392
7FDCEM6.6 ÅO=1-392
5VOXEM6.8 ÅO=1-392
3J9TEM6.9 ÅO=1-392
6O7WEM7.0 ÅO=1-392
3J9UEM7.6 ÅO=1-392
5VOZEM7.6 ÅO=1-392
5VOYEM7.9 ÅO=1-392
3J9VEM8.3 ÅO=1-392
6O7XEM8.7 ÅO=1-392

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