Apoptosis regulator BAX (BAX) is a 192-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q07812.
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The mean pLDDT of this model is 85.9 (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 | 59% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Plays a role in the mitochondrial apoptotic process (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:36361894, PubMed:8358790, PubMed:8521816). Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM) (PubMed:21458670). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis (PubMed:10772918,…
Homodimer. Forms higher oligomers under stress conditions. Forms heterooligomers with BAK (PubMed:29531808). Interacts with BCL2L11. Interaction with BCL2L11 promotes BAX oligomerization and association with mitochondrial membranes, with subsequent release of cytochrome c. Forms heterodimers with BCL2, BCL2L1 isoform Bcl-X(L), BCL2L2, MCL1 and A1 (PubMed:25609812). Interacts with SH3GLB1.…
Mitochondrion outer membrane, Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4ZIE | X-ray | 1.8 Å | A=1-166 |
| 5W60 | X-ray | 1.8 Å | A=1-192 |
| 4S0O | X-ray | 1.9 Å | A/B=1-192 |
| 5W5Z | X-ray | 2.0 Å | A=32-192 |
| 6EB6 | X-ray | 2.02 Å | A=1-192 |
| 8G1T | X-ray | 2.09 Å | A/B/C/D/E/F/G/H=53-128 |
| 8SRX | X-ray | 2.09 Å | B/D=53-128 |
| 6TRR | X-ray | 2.12 Å | B=50-77 |
| 4ZII | X-ray | 2.19 Å | A=1-170 |
| 4ZIG | X-ray | 2.2 Å | A=1-166 |
| 8SPF | X-ray | 2.2 Å | A/B/C/D/E/F=53-128 |
| 4BD2 | X-ray | 2.21 Å | A=1-171 |
| 7ADT | X-ray | 2.21 Å | C/U=50-77 |
| 4BD8 | X-ray | 2.22 Å | A/B/C/D=1-171 |
| 8SVK | X-ray | 2.25 Å | A/B/C/D=53-128 |
| 2G5B | X-ray | 2.3 Å | I/J/K/L=13-19 |
| 5W61 | X-ray | 2.3 Å | A=1-192 |
| 8SPE | X-ray | 2.3 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=53-128 |
| 4ZIF | X-ray | 2.4 Å | A=1-166 |
| 8SPZ | X-ray | 2.4 Å | A/B/C/D=53-128 |
Showing 20 of 37 experimental structures (best resolution first).
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