Ubiquitin-like modifier-activating enzyme ATG7 (ATG7) is a 630-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P38862.
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The mean pLDDT of this model is 91.9 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 78% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements…
Homodimer; homodimerization is required for ATP-binding (PubMed:11139573, PubMed:21193819, PubMed:29295865). Interacts with ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly-116' of ATG8 and with ATG12 through a thioester bond between Cys-507 and the C-terminal 'Gly-186' of ATG12 (PubMed:10233150, PubMed:11100732, PubMed:16874032, PubMed:18544538, PubMed:22055191). Also…
Cytoplasm, Preautophagosomal structure
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3T7H | X-ray | 1.6 Å | A/B=1-289 |
| 4GSJ | X-ray | 1.7 Å | A=1-289 |
| 3T7F | X-ray | 1.89 Å | A=1-289 |
| 3RUI | X-ray | 1.91 Å | A=293-630 |
| 3VH3 | X-ray | 2.0 Å | A=295-630 |
| 3T7G | X-ray | 2.08 Å | A/B=1-289 |
| 3RUJ | X-ray | 2.1 Å | A=1-294 |
| 5YEC | X-ray | 2.15 Å | A/C=295-630 |
| 3T7E | X-ray | 2.25 Å | A=289-630 |
| 3VH4 | X-ray | 2.65 Å | A=295-630 |
| 4GSL | X-ray | 2.7 Å | A/B=1-613 |
| 4GSK | X-ray | 2.9 Å | A/B=1-613 |
| 3VH1 | X-ray | 3.0 Å | A=1-595 |
| 3VH2 | X-ray | 3.3 Å | A=1-613 |
| 2LI5 | NMR | B=601-630 |
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