Pre-mRNA-processing-splicing factor 8 (PRPF8) is a 2335-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6P2Q9.
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The mean pLDDT of this model is 84.9 (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 | 44% |
| 70 to 90 | Confident: backbone generally right | 47% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes, both of the predominant U2-type spliceosome and the minor U12-type spliceosome (PubMed:10411133, PubMed:11971955, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30315277, PubMed:30705154, PubMed:30728453). Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome. Functions as a scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so…
Part of the U5 snRNP complex (PubMed:2527369, PubMed:2532307). Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (PubMed:16723661, PubMed:2479028, PubMed:26912367). Component of the U5.U4atac/U6atac snRNP complexes in U12-dependent…
Nucleus, Nucleus speckle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4JK8 | X-ray | 1.15 Å | A/B=1769-1990 |
| 4JKB | X-ray | 1.3 Å | A/B=1769-1990 |
| 4JKA | X-ray | 1.32 Å | A/B=1769-1990 |
| 4JK7 | X-ray | 1.4 Å | A/B=1769-1990 |
| 4JK9 | X-ray | 1.5 Å | A/B=1769-1990 |
| 4JKC | X-ray | 1.5 Å | A/B=1769-1990 |
| 4JKD | X-ray | 1.55 Å | A/B=1769-1990 |
| 4JKE | X-ray | 1.65 Å | A/B=1769-1990 |
| 4JKG | X-ray | 1.8 Å | A/B=1769-1990 |
| 4JKH | X-ray | 1.8 Å | A/B=1769-1990 |
| 3ENB | X-ray | 1.85 Å | A/B=1769-1990 |
| 3LRU | X-ray | 1.85 Å | A/B=1831-1990 |
| 3E9L | X-ray | 1.95 Å | A=1760-2016 |
| 4JKF | X-ray | 1.95 Å | A/B=1769-1990 |
| 8BCE | X-ray | 2.05 Å | J=2064-2320 |
| 8BC9 | X-ray | 2.3 Å | J=2064-2320 |
| 7PJH | X-ray | 2.35 Å | B=1758-2016 |
| 8BCC | X-ray | 2.35 Å | J=2064-2320 |
| 8BCB | X-ray | 2.38 Å | J=2064-2320 |
| 6S8Q | X-ray | 2.39 Å | J=2064-2320 |
Showing 20 of 100 experimental structures (best resolution first).
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