Caspase-1 (CASP1) is a 404-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P29466.
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The mean pLDDT of this model is 81.7 (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 | 57% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides (PubMed:15326478, PubMed:15498465, PubMed:1574116, PubMed:26375003, PubMed:32051255, PubMed:37993714, PubMed:7876192, PubMed:9334240). Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature…
Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (Caspase-1 subunit p20) and a 10 kDa (Caspase-1 subunit p10) subunit (PubMed:32109412, PubMed:32553275, PubMed:8044845, PubMed:9987822). May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and NLRP2 and whose function would be the activation of…
Cytoplasm, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8WRA | X-ray | 1.45 Å | A=120-404 |
| 1SC3 | X-ray | 1.8 Å | A=120-297, B=317-404 |
| 2H54 | X-ray | 1.8 Å | A=120-297, B=317-404 |
| 2HBQ | X-ray | 1.8 Å | A=120-297, B=317-404 |
| 3D6M | X-ray | 1.8 Å | A=120-297, B=317-404 |
| 6BZ9 | X-ray | 1.8 Å | A=120-297, B=317-404 |
| 6F6R | X-ray | 1.8 Å | A=118-297, B=317-404 |
| 1RWX | X-ray | 1.85 Å | A=120-297, B=317-404 |
| 2H4Y | X-ray | 1.9 Å | A=120-297, B=317-404 |
| 2HBZ | X-ray | 1.9 Å | A=120-297, B=317-404 |
| 3D6F | X-ray | 1.9 Å | A=120-297, B=317-404 |
| 6PZP | X-ray | 1.94 Å | A=120-297, B=317-404 |
| 1RWN | X-ray | 2.0 Å | A=120-297, B=317-404 |
| 2H4W | X-ray | 2.0 Å | A=120-297, B=317-404 |
| 3D6H | X-ray | 2.0 Å | A=120-297, B=317-404 |
| 3E4C | X-ray | 2.05 Å | A/B=104-404 |
| 1RWO | X-ray | 2.1 Å | A=120-297, B=317-404 |
| 1RWV | X-ray | 2.1 Å | A=120-297, B=317-404 |
| 1SC4 | X-ray | 2.1 Å | A=120-297, B=317-404 |
| 2H51 | X-ray | 2.1 Å | A=120-297, B=317-404 |
Showing 20 of 42 experimental structures (best resolution first).
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