Autophagy-related protein 16-1 (ATG16L1) is a 607-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q676U5.
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The mean pLDDT of this model is 83.9 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 70% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Plays an essential role in both canonical and non-canonical autophagy: interacts with ATG12-ATG5 to mediate the lipidation to ATG8 family proteins (MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP) (PubMed:23376921, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:27273576, PubMed:29317426, PubMed:30778222, PubMed:33909989). Acts as a molecular hub, coordinating autophagy pathways via distinct domains that support either canonical or non-canonical signaling (PubMed:29317426, PubMed:30778222). During canonical autophagy, interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to ATG8 proteins, to produce a membrane-bound activated form of…
Homodimer (PubMed:25484072). Homooligomer (By similarity). Heterooligomer with ATG16L2 (By similarity). Interacts with WIPI1 (PubMed:28561066). Interacts with WIPI2 (PubMed:24954904, PubMed:28561066). Interacts with RB1CC1; the interaction is required for ULK1 complex-dependent autophagy (PubMed:23262492, PubMed:23392225, PubMed:24954904). Interacts with ATG5 (PubMed:23202584, PubMed:24191030,…
Cytoplasm, Preautophagosomal structure membrane, Endosome membrane, Lysosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7F69 | X-ray | 1.5 Å | C=207-236 |
| 5NUV | X-ray | 1.55 Å | A=303-607 |
| 9J54 | X-ray | 1.61 Å | B/D=235-247 |
| 7XFR | X-ray | 1.76 Å | B/D=124-188 |
| 9JF2 | X-ray | 1.76 Å | C/D=235-247 |
| 4NAW | X-ray | 2.2 Å | C/G/K/O=11-43 |
| 4GDK | X-ray | 2.7 Å | C/F=11-43 |
| 4TQ0 | X-ray | 2.7 Å | B/D/F=1-69 |
| 8ZQG | X-ray | 2.77 Å | C/D=124-188 |
| 4GDL | X-ray | 2.88 Å | C=11-43 |
| 5D7G | X-ray | 3.0 Å | B/D/F/H=1-69 |
| 7W36 | X-ray | 3.0 Å | B=13-33 |
| 5NPV | X-ray | 3.1 Å | B/D=11-307 |
| 5NPW | X-ray | 3.1 Å | B/D/F/H=11-307 |
| 5ZYX | NMR | A=12-31 |
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