Apoptosis regulator Bcl-2 (BCL2) is a 239-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10415.
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The mean pLDDT of this model is 72.0 (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 | 21% |
| 50 to 70 | Low: treat with caution | 16% |
| Below 50 | Very low: often disordered regions | 25% |
What pLDDT means and how to read it
Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells (PubMed:1508712, PubMed:8183370). Regulates cell death by controlling the mitochondrial membrane permeability (PubMed:11368354). Appears to function in a feedback loop system with caspases (PubMed:11368354). Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (PubMed:11368354). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (PubMed:18570871, PubMed:20889974, PubMed:21358617).…
Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity (PubMed:25609812, PubMed:8183370). Part of a complex composed of SEPTIN4 isoform ARTS, XIAP and BCL2, within the complex interacts (via BH3 domain) with SEPTIN4 isoform ARTS and XIAP, SEPTIN4 isoform ARTS acts as a…
Mitochondrion outer membrane, Nucleus membrane, Endoplasmic reticulum membrane, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8HTS | X-ray | 1.25 Å | A=1-207 |
| 6GL8 | X-ray | 1.4 Å | A=9-206 |
| 6QGG | X-ray | 1.5 Å | A=10-203 |
| 8HTR | X-ray | 1.6 Å | A=1-207 |
| 6O0K | X-ray | 1.62 Å | A=1-34, A=66-207 |
| 9O14 | X-ray | 1.73 Å | A=1-34, A=66-207 |
| 9O16 | X-ray | 1.73 Å | A=1-34, A=66-207 |
| 5VAU | X-ray | 1.75 Å | A/B/C/D=1-207 |
| 6O0M | X-ray | 1.75 Å | A=1-34, A=66-207 |
| 8VWX | X-ray | 1.77 Å | A=10-34, A=66-207 |
| 5VAY | X-ray | 1.8 Å | A/B/C/D=1-34, A/B/C/D=66-207 |
| 6O0P | X-ray | 1.8 Å | A=1-34, A=66-207 |
| 6QGK | X-ray | 1.8 Å | A=10-203 |
| 8HOG | X-ray | 1.8 Å | A=5-207 |
| 7YA5 | X-ray | 1.85 Å | A=1-34, A=92-207 |
| 4LXD | X-ray | 1.9 Å | A=1-34, A=92-207 |
| 6QG8 | X-ray | 1.9 Å | A=10-203 |
| 6QGJ | X-ray | 1.9 Å | A=10-203 |
| 8HOH | X-ray | 1.9 Å | A=5-207 |
| 9O15 | X-ray | 1.99 Å | A/C/E/G/I/K=1-34, A/C/E/G/I/K=66-207 |
Showing 20 of 55 experimental structures (best resolution first).
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