Caspase-7 (CASP7) is a 303-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P55210.
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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 | 66% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
Thiol protease involved in different programmed cell death processes, such as apoptosis, pyroptosis or granzyme-mediated programmed cell death, by proteolytically cleaving target proteins (PubMed:11257230, PubMed:11257231, PubMed:11701129, PubMed:15314233, PubMed:16916640, PubMed:17646170, PubMed:18723680, PubMed:19581639, PubMed:8521391, PubMed:8567622, PubMed:8576161, PubMed:9070923). Has a marked preference for Asp-Glu-Val-Asp (DEVD) consensus sequences, with some plasticity for alternate non-canonical sequences (PubMed:12824163, PubMed:15314233, PubMed:17697120, PubMed:19581639, PubMed:20566630, PubMed:23650375, PubMed:23897474, PubMed:27032039). Its involvement in the different…
Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit (PubMed:11701129, PubMed:11752425, PubMed:16916640, PubMed:20566630). Interacts with XIAP (via its second BIR domain); inhibiting CASP7 activity (PubMed:11257230, PubMed:11257231, PubMed:16916640). Interacts with BIRC6/bruce (PubMed:15200957). Interacts with ATXN3…
Cytoplasm, cytosol, Nucleus, Secreted, extracellular space
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4JR2 | X-ray | 1.65 Å | A/B=57-303 |
| 4JB8 | X-ray | 1.7 Å | A=24-198, B=207-303 |
| 2QL9 | X-ray | 2.14 Å | A/C=24-196, B/D=207-303 |
| 4JR1 | X-ray | 2.15 Å | A/B=57-303 |
| 5K20 | X-ray | 2.2 Å | A/C=1-198, B/D=199-303 |
| 2QLB | X-ray | 2.25 Å | A/C=24-196, B/D=207-303 |
| 4LSZ | X-ray | 2.26 Å | A/C=24-198, B/D=207-303 |
| 4ZVR | X-ray | 2.3 Å | A/C=1-198, B/D=199-303 |
| 2QL5 | X-ray | 2.34 Å | A/C=24-196, B/D=207-303 |
| 1F1J | X-ray | 2.35 Å | A/B=1-303 |
| 6CL2 | X-ray | 2.35 Å | A/C=1-198, B/D=199-303 |
| 1I4O | X-ray | 2.4 Å | A/B=24-303 |
| 2QL7 | X-ray | 2.4 Å | A/C=24-196, B/D=207-303 |
| 1I51 | X-ray | 2.45 Å | A/C=51-198, B/D=199-303 |
| 3EDR | X-ray | 2.45 Å | A/C=24-196, B/D=207-303 |
| 6X8L | X-ray | 2.45 Å | A/B=1-198, C/D=199-303 |
| 3IBF | X-ray | 2.5 Å | A/C=24-196, B/D=207-303 |
| 4ZVP | X-ray | 2.5 Å | A/C=1-198, B/D=199-303 |
| 4ZVQ | X-ray | 2.5 Å | A/C=1-198, B/D=199-303 |
| 4ZVS | X-ray | 2.5 Å | A/C=1-198, B/D=199-303 |
Showing 20 of 47 experimental structures (best resolution first).
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