O00410: Importin-5 (IPO5)

Importin-5 (IPO5) is a 1097-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00410.

Gene
IPO5
Organism
Homo sapiens
Length
1097 residues
Mean pLDDT
92.1
Model
AF-O00410-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.1 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate81%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin 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 the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP-…

Subunit structure

Interacts with RPS7 and RPL5 (PubMed:9687515). Interacts with RPL23A (via BIB domain) (PubMed:11682607, PubMed:9687515). Interacts with H2A, H2B, H3 and H4 histones (By similarity). Interacts with CPEB3; this mediates CPEB3 nuclear import following neuronal stimulation which enhances the interaction in a RAN-regulated manner (PubMed:22730302). Interacts with AIFM2; this interaction likely…

Subcellular location

Cytoplasm, Nucleus, Nucleus, nucleolus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6XTEX-ray2.27 ÅA=4-1097
6XU2X-ray2.83 ÅA=1-1097
9IM6EM3.21 ÅA=1-1097

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