Importin subunit alpha-1 (Kpna2) is a 529-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P52293.
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The mean pLDDT of this model is 86.9 (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 | 78% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1 (PubMed:21690087). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:21690087). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin.…
Heterodimer; with KPNB1 (By similarity). Component of a complex containing CSE1L, RAN and KPNA2 (By similarity). Interacts directly with CSE1L (By similarity). Interacts with PLAG1 (By similarity). Interacts with APEX1 (via N-terminus) (By similarity). Interacts with FRG1 (via N-terminus) (By similarity). Interacts with ARL4A, CTNNBL1 and NBN (By similarity). Interacts with ANP32E…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4UAF | X-ray | 1.7 Å | B=69-529 |
| 5CTT | X-ray | 1.7 Å | A=72-497 |
| 6IUA | X-ray | 1.7 Å | A=72-498 |
| 6K06 | X-ray | 1.75 Å | C=70-498 |
| 8HE0 | X-ray | 1.8 Å | A=72-498 |
| 4YI0 | X-ray | 1.81 Å | C=70-529 |
| 7RG1 | X-ray | 1.85 Å | A=70-529 |
| 4MZ6 | X-ray | 1.88 Å | E=70-528 |
| 3UL1 | X-ray | 1.9 Å | B=70-529 |
| 5D5K | X-ray | 1.9 Å | C=70-529 |
| 5UMZ | X-ray | 1.9 Å | B=70-528 |
| 6IU7 | X-ray | 1.9 Å | A=72-498 |
| 8FUA | X-ray | 1.9 Å | A=70-529 |
| 8HE3 | X-ray | 1.9 Å | A=72-498 |
| 8QXX | X-ray | 1.9 Å | A=70-529 |
| 5HUW | X-ray | 1.95 Å | C=2-529 |
| 7RFZ | X-ray | 1.95 Å | A=70-529 |
| 4U5U | X-ray | 1.96 Å | A=72-497 |
| 7JK7 | X-ray | 1.96 Å | B=62-529 |
| 4U5V | X-ray | 1.97 Å | A=72-497 |
Showing 20 of 151 experimental structures (best resolution first).
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