Importin subunit beta-1 (KPNB1) is a 876-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14974.
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The mean pLDDT of this model is 94.8 (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 | 90% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). Acting autonomously, serves itself as NLS receptor (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG…
Forms a complex with an importin alpha subunit (PubMed:20818336, PubMed:8617227, PubMed:8692944). Interacts with XPO1 (PubMed:10209022). Forms a heterodimer with IPO7 (PubMed:10209022, PubMed:10228156, PubMed:9687515). The KPNB1/IPO7 heterodimer interacts with H1 histone (PubMed:10228156). Interacts with SNUPN (PubMed:10209022, PubMed:18187419, PubMed:20476751, PubMed:9670026). Interacts with…
Cytoplasm, Nucleus envelope
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1IBR | X-ray | 2.3 Å | B/D=1-462 |
| 1QGR | X-ray | 2.3 Å | A=1-876 |
| 2P8Q | X-ray | 2.35 Å | A=1-876 |
| 1QGK | X-ray | 2.5 Å | A=1-876 |
| 3W5K | X-ray | 2.6 Å | A=1-876 |
| 9N85 | EM | 2.6 Å | A=1-876 |
| 1F59 | X-ray | 2.8 Å | A/B=1-442 |
| 1O6O | X-ray | 2.8 Å | A/B/C=1-442 |
| 1O6P | X-ray | 2.8 Å | A/B=1-442 |
| 2QNA | X-ray | 2.84 Å | A=127-875 |
| 1M5N | X-ray | 2.9 Å | S=1-485 |
| 3LWW | X-ray | 3.15 Å | A/C=1-876 |
| 2Q5D | X-ray | 3.2 Å | A/B=1-876 |
| 9BFC | EM | 3.2 Å | H=1-876 |
| 9YB5 | EM | 3.2 Å | B=2-459 |
| 9BAW | EM | 3.3 Å | A=1-876 |
| 9N86 | EM | 3.3 Å | A=1-876 |
| 9N87 | EM | 3.4 Å | A=1-876 |
| 9B4Y | EM | 3.74 Å | A=1-876 |
| 8GCN | EM | 3.95 Å | A=1-876 |
Showing 20 of 23 experimental structures (best resolution first).
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