Bcl-2-like protein 1 (BCL2L1) is a 233-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q07817.
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The mean pLDDT of this model is 72.5 (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 | 39% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 31% |
What pLDDT means and how to read it
Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis
Homodimer. Interacts with BCL2L11 (By similarity). Interacts with BAD. Interacts with PGAM5. Interacts with HEBP2. Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with p53/TP53. Interacts with ATP5F1A and ATP5F1B; the interactions mediate the association of isoform Bcl-X(L) with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase. Interacts with VDAC1…
Mitochondrion inner membrane, Mitochondrion outer membrane, Mitochondrion matrix, Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane, Cytoplasm, cytosol, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Nucleus membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7JGW | X-ray | 1.3 Å | A=1-209 |
| 3SP7 | X-ray | 1.4 Å | A=1-209 |
| 7YAA | X-ray | 1.4 Å | A=1-196 |
| 7LH7 | X-ray | 1.41 Å | A/B=1-25, A/B=83-209 |
| 4QVF | X-ray | 1.53 Å | A=1-209 |
| 4A1U | X-ray | 1.54 Å | A=1-209 |
| 6VWC | X-ray | 1.6 Å | A/B=1-25, A/B=83-209 |
| 6O0K | X-ray | 1.62 Å | A=29-44 |
| 3SPF | X-ray | 1.7 Å | A=1-209 |
| 5FMK | X-ray | 1.73 Å | A=1-209 |
| 9O14 | X-ray | 1.73 Å | A=29-44 |
| 9O16 | X-ray | 1.73 Å | A=29-44 |
| 6O0M | X-ray | 1.75 Å | A=29-44 |
| 4BPK | X-ray | 1.76 Å | A/B=1-209 |
| 8VWX | X-ray | 1.77 Å | A=29-44 |
| 3FDL | X-ray | 1.78 Å | A=1-209 |
| 6ST2 | X-ray | 1.79 Å | A/B=1-209 |
| 2YQ6 | X-ray | 1.8 Å | A=1-209 |
| 4TUH | X-ray | 1.8 Å | A/B/C/D/E/F/G/H=1-209 |
| 5VAY | X-ray | 1.8 Å | A/B/C/D=29-44 |
Showing 20 of 118 experimental structures (best resolution first).
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