Beclin-1 (BECN1) is a 450-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14457.
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The mean pLDDT of this model is 76.6 (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 | 38% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Plays a central role in autophagy (PubMed:18570871, PubMed:21358617, PubMed:23184933, PubMed:23974797, PubMed:25484083, PubMed:28445460, PubMed:37776275). Acts as a core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abscission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20208530, PubMed:20643123, PubMed:23974797, PubMed:26783301).…
A homodimeric form is proposed to exist; this metastable form readily transits to ATG14- or UVRAG-containing complexes with BECN1:UVRAG being more stable than BECN1:ATG14 (By similarity). Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex the core of which is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating with…
Cytoplasm, Golgi apparatus, trans-Golgi network membrane, Endosome membrane, Endoplasmic reticulum membrane, Mitochondrion membrane, Endosome, Cytoplasmic vesicle, autophagosome, Mitochondrion, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6HOI | X-ray | 1.14 Å | F/G=93-102 |
| 5HHE | X-ray | 1.46 Å | A/D=175-265 |
| 6HOJ | X-ray | 1.51 Å | A/B/C=93-105 |
| 4DDP | X-ray | 1.55 Å | A=241-450 |
| 6HOK | X-ray | 1.61 Å | A=93-105 |
| 5VAU | X-ray | 1.75 Å | E/F/G/H=105-130 |
| 5VAY | X-ray | 1.8 Å | E/F/G/H=105-130 |
| 5EFM | X-ray | 1.95 Å | A=141-171 |
| 5VAX | X-ray | 2.0 Å | E/F/G/H=105-130 |
| 4MI8 | X-ray | 2.1 Å | C/D=107-130 |
| 6DCO | X-ray | 2.2 Å | C/D=105-130 |
| 6DCN | X-ray | 2.44 Å | C/D=105-130 |
| 2P1L | X-ray | 2.5 Å | B/D/F/H=107-135 |
| 3DVU | X-ray | 2.5 Å | C/D=105-130 |
| 9MHF | EM | 2.73 Å | D=1-450 |
| 9MHG | EM | 3.2 Å | D=1-450 |
| 9ZPD | EM | 3.38 Å | D/E=1-450 |
| 13BV | EM | 3.77 Å | D=1-450 |
| 9ZPC | EM | 3.83 Å | D=1-450 |
| 9MHH | EM | 4.5 Å | D=1-450 |
Showing 20 of 23 experimental structures (best resolution first).
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