Q9QZQ1: Afadin (Afdn)

Afadin (Afdn) is a 1820-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9QZQ1.

Gene
Afdn
Organism
Mus musculus
Length
1820 residues
Mean pLDDT
63.7
Model
AF-Q9QZQ1-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.7 (low 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 accurate26%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions40%

What pLDDT means and how to read it

Function

Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs) (By similarity). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton (By similarity). May play a key role in the organization of epithelial structures of the embryonic ectoderm (PubMed:10477764). Essential for the organization of adherens junctions (By similarity)

Subunit structure

Homodimer. Interacts with F-actin, nectin and NECTIN3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadin does not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1, RIT2, NRXN1 and BCR (By similarity). Interacts with ADAM10; the interaction locks ADAM10 at adherens junctions following ADAM10 recruitment to…

Subcellular location

Cell junction, adherens junction

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6AMBX-ray2.5 ÅB=38-136
3AXAX-ray2.78 ÅA/B=1003-1095
9DVAEM3.1 ÅG=1393-1602
1WLNNMRA=381-502
1WXANMRA=246-348

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