14-3-3 protein sigma (SFN) is a 248-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P31947.
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The mean pLDDT of this model is 92.9 (very high 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 | 85% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010). Binding generally results in the modulation of the activity of the binding partner (PubMed:15731107, PubMed:22634725, PubMed:28202711, PubMed:37797010). Promotes cytosolic retention of GBP1 GTPase by binding to phosphorylated GBP1, thereby inhibiting the innate immune response (PubMed:37797010). Also acts as a TP53/p53-regulated…
Homodimer (PubMed:28202711). Interacts with KRT17 and SAMSN1 (By similarity). Forms heterodimers with YWHAG, YWHAB or YWHAQ (By similarity). Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29 and VPS35 (PubMed:15282546). Interacts with GAB2 (PubMed:19172738). Interacts with SRPK2 (PubMed:19592491). Interacts with COPS6 (PubMed:21625211). Interacts with COP1; this interaction leads to…
Cytoplasm, Nucleus, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3IQU | X-ray | 1.05 Å | A=1-231 |
| 7AZ2 | X-ray | 1.08 Å | A=1-248 |
| 6HMT | X-ray | 1.1 Å | A=1-231 |
| 7BAA | X-ray | 1.1 Å | A=1-231 |
| 8BZC | X-ray | 1.1 Å | A=1-231 |
| 8BZW | X-ray | 1.1 Å | A=1-231 |
| 8C04 | X-ray | 1.1 Å | A=1-231 |
| 9GG8 | X-ray | 1.1 Å | A=1-231 |
| 8ANC | X-ray | 1.11 Å | A=1-231 |
| 6G6X | X-ray | 1.13 Å | A=1-231 |
| 6NV2 | X-ray | 1.13 Å | A=1-231 |
| 6Y1J | X-ray | 1.13 Å | A=1-248 |
| 3IQJ | X-ray | 1.15 Å | A=1-231 |
| 3MHR | X-ray | 1.15 Å | A=1-231 |
| 7AZ1 | X-ray | 1.15 Å | A=1-248 |
| 7B9R | X-ray | 1.15 Å | A=1-231 |
| 7B9T | X-ray | 1.15 Å | A=1-231 |
| 7NFW | X-ray | 1.19 Å | A=1-248 |
| 3IQV | X-ray | 1.2 Å | A=1-231 |
| 5MHC | X-ray | 1.2 Å | A=1-231 |
Showing 20 of 524 experimental structures (best resolution first).
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