T-complex protein 1 subunit theta (CCT8) is a 548-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P50990.
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The mean pLDDT of this model is 87.7 (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 | 36% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638)
Component of the chaperonin-containing T-complex (TRiC), a hexadecamer composed of two identical back-to-back stacked rings enclosing a protein folding chamber (PubMed:20080638, PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). Each ring is made up of eight different subunits: TCP1/CCT1, CCT2, CCT3, CCT4, CCT5, CCT6A/CCT6, CCT7, CCT8 (PubMed:36493755, PubMed:35449234,…
Cytoplasm, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cytoskeleton, cilium basal body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7NVL | EM | 2.5 Å | Q/q=1-548 |
| 8SH9 | EM | 2.7 Å | Q/q=2-539 |
| 8SHE | EM | 2.8 Å | Q/q=2-539 |
| 8SHG | EM | 2.8 Å | Q/q=2-539 |
| 8SHN | EM | 2.8 Å | Q/q=2-539 |
| 7TTT | EM | 2.9 Å | B=1-547 |
| 8SG9 | EM | 2.9 Å | Q/q=2-539 |
| 8SGC | EM | 2.9 Å | Q/q=2-539 |
| 8SGL | EM | 2.9 Å | Q/q=2-539 |
| 8SHD | EM | 2.9 Å | Q/q=2-539 |
| 8SHQ | EM | 2.9 Å | Q/q=2-539 |
| 9NOQ | EM | 2.9 Å | Q/q=1-548 |
| 9NRH | EM | 2.9 Å | Q/q=1-548 |
| 7NVN | EM | 3.0 Å | Q/q=1-548 |
| 7TRG | EM | 3.0 Å | B=1-547 |
| 8SG8 | EM | 3.0 Å | Q/q=2-539 |
| 8SHA | EM | 3.0 Å | Q/q=2-539 |
| 8SHF | EM | 3.0 Å | Q/q=2-539 |
| 8SHL | EM | 3.0 Å | Q/q=2-539 |
| 8SHO | EM | 3.0 Å | Q/q=2-539 |
Showing 20 of 64 experimental structures (best resolution first).
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