Splicing factor 3B subunit 1 (SF3B1) is a 1304-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75533.
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The mean pLDDT of this model is 74.8 (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 | 45% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 24% |
What pLDDT means and how to read it
Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, PubMed:32494006, PubMed:34822310, PubMed:36104565). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:32494006, PubMed:34822310, PubMed:36104565). Within the 17S U2 SnRNP complex, SF3B1 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding…
Component of the 17S U2 SnRNP complex, a ribonucleoprotein complex that contains small nuclear RNA (snRNA) U2 and a number of specific proteins (PubMed:30567737, PubMed:32494006, PubMed:34822310, PubMed:36797247). Part of the SF3B subcomplex of the 17S U2 SnRNP complex (PubMed:12234937, PubMed:12738865, PubMed:27720643, PubMed:28541300). SF3B associates with the splicing subcomplex SF3A and a…
Nucleus, Nucleus speckle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4OZ1 | X-ray | 1.74 Å | C=333-342 |
| 7SN6 | X-ray | 1.8 Å | C/D=333-351 |
| 6N3E | X-ray | 1.89 Å | B=291-297 |
| 6N3F | X-ray | 2.1 Å | D=336-339 |
| 2PEH | X-ray | 2.11 Å | C/D=333-342 |
| 7Q4O | EM | 2.2 Å | A=1-1304 |
| 7Q4P | EM | 2.2 Å | A=1-1304 |
| 7Q3L | EM | 2.3 Å | A=1-1304 |
| 3LQV | X-ray | 2.38 Å | P/Q=377-415 |
| 7B9C | X-ray | 2.4 Å | C=453-1304 |
| 2F9D | X-ray | 2.5 Å | P/Q=373-415 |
| 7EVO | EM | 2.5 Å | 1=1-1304 |
| 7EVN | EM | 2.6 Å | C=452-1304 |
| 8H6L | EM | 2.6 Å | 2G=1-1304 |
| 8H6K | EM | 2.7 Å | 2G=1-1304 |
| 8HK1 | EM | 2.7 Å | 1=1-1304 |
| 7DVQ | EM | 2.89 Å | 1=1-1304 |
| 2F9J | X-ray | 3.0 Å | P/Q=381-415 |
| 7B0I | X-ray | 3.0 Å | C=453-1304 |
| 7B91 | X-ray | 3.0 Å | C=453-1304 |
Showing 20 of 71 experimental structures (best resolution first).
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