Microtubule-associated protein 1 light chain 3 beta (MAP1LC3B) is a 125-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9GZQ8.
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The mean pLDDT of this model is 91.4 (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 | 16% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20418806, PubMed:23209295, PubMed:28017329). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:23209295, PubMed:28017329). In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria (PubMed:22922758). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is…
3 different light chains, LC1 (a cleavage product of MAP1B), LC2 (a cleavage product of MAP1A) and LC3 (produced by one of the MAP1LC3 genes), can associate with the MAP1A or MAP1B heavy chains (By similarity). Interacts at microtubules with CABP1 (via EF-hands 1 and 2) but not with calmodulin (PubMed:15095872). Interacts with FYCO1 (via C-terminus) (PubMed:20100911, PubMed:24089205). Interacts…
Cytoplasmic vesicle, autophagosome membrane, Endomembrane system, Mitochondrion membrane, Cytoplasm, cytoskeleton, Cytoplasmic vesicle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8Q53 | X-ray | 1.36 Å | A=1-125 |
| 6LAN | X-ray | 1.41 Å | A=2-125 |
| 5D94 | X-ray | 1.53 Å | A=1-125 |
| 5MS5 | X-ray | 1.53 Å | A/B=2-119 |
| 2ZJD | X-ray | 1.56 Å | A/C=1-125 |
| 7GAG | X-ray | 1.59 Å | A=1-120 |
| 7GAU | X-ray | 1.59 Å | A=1-120 |
| 3VTU | X-ray | 1.6 Å | A=2-119 |
| 7ELG | X-ray | 1.6 Å | A=2-119 |
| 8Q7K | X-ray | 1.6 Å | A/B=1-125 |
| 7GAP | X-ray | 1.68 Å | A=1-120 |
| 7GAO | X-ray | 1.69 Å | A=1-120 |
| 3VTV | X-ray | 1.7 Å | A=2-119 |
| 5XAC | X-ray | 1.7 Å | A/B/C/D=2-120 |
| 7GAM | X-ray | 1.75 Å | A=1-120 |
| 8YV6 | X-ray | 1.75 Å | A=1-125 |
| 7GAK | X-ray | 1.77 Å | A=1-120 |
| 7GAF | X-ray | 1.84 Å | A=1-120 |
| 7GAD | X-ray | 1.86 Å | A=1-120 |
| 7GA8 | X-ray | 1.87 Å | A=1-120 |
Showing 20 of 49 experimental structures (best resolution first).
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