P52294: Importin subunit alpha-5 (KPNA1)

Importin subunit alpha-5 (KPNA1) is a 538-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P52294.

Gene
KPNA1
Organism
Homo sapiens
Length
538 residues
Mean pLDDT
86.2
Model
AF-P52294-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.2 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate76%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1 (PubMed:27713473, PubMed:7892216, PubMed:8692858). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:27713473, PubMed:7892216, PubMed:8692858). 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 (PubMed:27713473, PubMed:7892216). At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta…

Subunit structure

Heterodimer; with KPNB1 (PubMed:7604027, PubMed:7892216, PubMed:8692858). Interacts with ANP32E (By similarity). Interacts with ZIC3 (By similarity). Interacts with NSMF; the interaction occurs in a calcium-independent manner after synaptic NMDA receptor stimulation and is required for nuclear import of NSMF but is competed by CABP1 (By similarity). Interacts with APEX1 (PubMed:15942031).…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
2JDQX-ray2.2 ÅA/B=66-512
4B18X-ray2.52 ÅA=66-512
3TJ3X-ray2.7 ÅA/B=66-512
6WX9X-ray2.8 ÅA=73-538

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