P41807: V-type proton ATPase subunit H (VMA13)

V-type proton ATPase subunit H (VMA13) is a 478-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P41807.

Gene
VMA13
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
478 residues
Mean pLDDT
84.8
Model
AF-P41807-F1 v6
Model created
1 Aug 2025
PDB structures
23

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 84.8 (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 accurate43%
70 to 90Confident: backbone generally right48%
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:27295975, PubMed:8349704). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:27295975, PubMed:8349704). This subunit is essential for activity, but not assembly, of the enzyme complex (PubMed:27295975, PubMed:8349704). This subunit is also required for silencing the ATPase activity of V-ATPase when V1 is detached from V0 (PubMed:27295975)

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:18055462, PubMed:25971514, PubMed:27295975, PubMed:8349704). Interacts with YND1 (PubMed:10954728)

Subcellular location

Vacuole membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9COPEM2.7 ÅP=1-478
1HO8X-ray2.95 ÅA=1-478
7TMOEM3.3 ÅP=1-478
7TMPEM3.3 ÅP=1-478
7TMQEM3.3 ÅP=1-478
7TMMEM3.5 ÅP=1-478
7TMREM3.5 ÅP=1-478
7TMSEM3.8 ÅP=1-478
7TMTEM3.8 ÅP=1-478
7FDAEM4.2 ÅP=1-359
7FDBEM4.8 ÅP=1-359
5D80X-ray6.2 ÅH/h=1-478
6O7VEM6.6 ÅP=1-478
7FDCEM6.6 ÅP=1-359
5VOXEM6.8 ÅP=1-478
3J9TEM6.9 ÅP=1-478
5BW9X-ray7.0 ÅH/h=1-478
6O7WEM7.0 ÅP=1-478
3J9UEM7.6 ÅP=1-478
5VOZEM7.6 ÅP=1-478

Showing 20 of 23 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.