Protein lgg-1 (lgg-1) is a 123-residue protein from Caenorhabditis elegans. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q09490.
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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 | 87% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes) (PubMed:26687600, PubMed:37395461). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy (PubMed:21802374, PubMed:26687600, PubMed:37395461). Recruits lipidated-lgg-2 to maturing autophagosomes (PubMed:12958363, PubMed:20523114, PubMed:26687600). Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation (PubMed:26687600). In…
Interacts with sepa-1 (via the LIR motifs); the interaction is direct (PubMed:19167332, PubMed:26687600). Interacts with allo-1 (via the LIR motif) (PubMed:29255173). Interacts with sqst-1 (via the LIR motifs); the interaction is direct (PubMed:26687600). Both lipidated and unlipidated forms interact with epg-7 (via the LIR motif); the interaction is direct (PubMed:26687600). Interacts with…
Preautophagosomal structure, Cytoplasmic vesicle, autophagosome, Cytoplasmic vesicle, autophagosome membrane, Lysosome lumen, Mitochondrion, Cytoplasm, Cytoplasmic vesicle, phagosome membrane, Cell membrane, Cell projection, dendrite, Perikaryon
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5AZF | X-ray | 1.6 Å | A/B=1-116 |
| 8TGF | X-ray | 1.6 Å | A=1-123 |
| 5AZG | X-ray | 1.81 Å | A/B=1-116 |
| 8TGX | X-ray | 2.62 Å | A=1-123 |
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