Q4KMG0: Cell adhesion molecule-related/down-regulated by oncogenes (CDON)

Cell adhesion molecule-related/down-regulated by oncogenes (CDON) is a 1287-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q4KMG0.

Gene
CDON
Organism
Homo sapiens
Length
1287 residues
Mean pLDDT
62.0
Model
AF-Q4KMG0-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.0 (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 accurate10%
70 to 90Confident: backbone generally right42%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions37%

What pLDDT means and how to read it

Function

Together with BOC, forms a coreceptor required for sonic hedgehog (SHH) handoff to its patched receptor (PTCH1 or PTCH2), thereby allowing activation of the smoothened signaling pathway (By similarity). Binds to the dually lipid-modified Sonic hedgehog protein N-product (ShhN) downstream of SCUBE2 carrier and promotes its release to GAS1 (By similarity). ShhN is then directly transferred to patched receptor by GAS1 (By similarity). May also mediate cell-cell interactions between muscle precursor cells, promoting differentiation of myogenic cells (By similarity)

Subunit structure

Heterodimer; heterodimerizes with BOC to form a functional complex (By similarity). Component of a complex composed of BOC, CDON, NEO1, cadherins and CTNNB1 (By similarity). Interacts with NTN3 (By similarity). Interacts with PTCH1 (By similarity). Interacts with GAS1 (By similarity). Interacts with DHH, IHH and SHH (PubMed:18794898, PubMed:20519495)

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3N1FX-ray1.6 ÅC/D=826-924
3D1MX-ray1.7 ÅC/D=826-924
3N1QX-ray2.89 ÅC/D/F=826-924

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