P22203: V-type proton ATPase subunit E (VMA4)

V-type proton ATPase subunit E (VMA4) is a 233-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P22203.

Gene
VMA4
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
233 residues
Mean pLDDT
90.1
Model
AF-P22203-F1 v6
Model created
1 Aug 2025
PDB structures
24

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.1 (very high 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 accurate67%
70 to 90Confident: backbone generally right29%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions2%

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:8416931). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:2145285, PubMed:8416931)

Subunit structure

Homodimer (PubMed:8626613). 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:2145285, PubMed:25971514, PubMed:27295975, PubMed:8416931). Interacts with VMA5; the interaction is direct (PubMed:15751969). Interacts…

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 ÅI/K=1-233
4EFAX-ray2.82 ÅE=1-233
4DL0X-ray2.9 ÅE/J=1-233
7TMOEM3.3 ÅG/I/K=1-233
7TMPEM3.3 ÅG/I/K=1-233
7TMQEM3.3 ÅG/I/K=1-233
7TMMEM3.5 ÅG/I/K=1-233
7TMREM3.5 ÅG/I/K=1-233
7FDEEM3.8 ÅG/I/K=1-233
7FDAEM4.2 ÅG/I/K=1-233
7FDBEM4.8 ÅG/I/K=1-233
5D80X-ray6.2 ÅI/K/M/i/k/m=1-233
6O7VEM6.6 ÅG/I/K=1-233
7FDCEM6.6 ÅG/I/K=1-233
5VOXEM6.8 ÅG/I/K=1-233
3J9TEM6.9 ÅG/I/K=1-233
5BW9X-ray7.0 ÅI/K/M/i/k/m=1-233
6O7WEM7.0 ÅG/I/K=1-233
3J9UEM7.6 ÅG/I/K=1-233
5VOZEM7.6 ÅG/I/K=1-233

Showing 20 of 24 experimental structures (best resolution first).

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