Galectin-8 (LGALS8) is a 317-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00214.
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The mean pLDDT of this model is 90.7 (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 | 82% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy (PubMed:22246324, PubMed:28077878). Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture (PubMed:22246324, PubMed:28077878). Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52 (PubMed:22246324, PubMed:28077878). Required to restrict infection of bacterial invasion such as S.typhimurium (PubMed:22246324). Also required to restrict infection of Picornaviridae…
Homodimer (PubMed:21288902, Ref.15). Interacts with CALCOCO2/NDP52 (PubMed:22246324). Interacts with PDPN; the interaction is glycosylation-dependent; may participate in connection of the lymphatic endothelium to the surrounding extracellular matrix
Cytoplasmic vesicle, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5GZC | X-ray | 1.08 Å | A=7-158 |
| 9FYJ | X-ray | 1.08 Å | A/B=4-156 |
| 5GZD | X-ray | 1.19 Å | A=7-154 |
| 9FXZ | X-ray | 1.3 Å | A/B=1-317 |
| 5GZE | X-ray | 1.32 Å | A=7-154 |
| 3AP9 | X-ray | 1.33 Å | A=1-154 |
| 6Z6Y | X-ray | 1.34 Å | A=5-160 |
| 4BMB | X-ray | 1.35 Å | A=4-153 |
| 7ALS | X-ray | 1.35 Å | A/B=4-158 |
| 7P1M | X-ray | 1.52 Å | A/B=6-156 |
| 3AP7 | X-ray | 1.53 Å | A=1-154 |
| 3AP6 | X-ray | 1.58 Å | A/B/C/D=1-154 |
| 5T7U | X-ray | 1.58 Å | A=1-155 |
| 6W4Z | X-ray | 1.59 Å | A/B=2-154 |
| 7AEN | X-ray | 1.6 Å | A/B=7-156 |
| 8HL9 | X-ray | 1.6 Å | A=171-317 |
| 9KH4 | X-ray | 1.75 Å | A=4-153 |
| 5T7S | X-ray | 1.9 Å | A=1-155 |
| 2YV8 | X-ray | 1.92 Å | A=1-151 |
| 3AP5 | X-ray | 1.92 Å | A=1-154 |
Showing 20 of 39 experimental structures (best resolution first).
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