Disks large homolog 4 (Dlg4) is a 724-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P31016.
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The mean pLDDT of this model is 77.7 (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 | 53% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 20% |
What pLDDT means and how to read it
Postsynaptic scaffolding protein that plays a critical role in synaptogenesis and synaptic plasticity by providing a platform for the postsynaptic clustering of crucial synaptic proteins (PubMed:15317815, PubMed:15358863, PubMed:19596852, PubMed:20628354, PubMed:23300088, PubMed:26679993). Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the…
Interacts through its PDZ domains with ANO2 and NETO1 (By similarity). Interacts with KCNJ4 (PubMed:11997254). Interacts through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C and GRIN2D (PubMed:7569905). Interacts with ERBB4 (By similarity). Interacts with KCNA1, KCNA2, KCNA3 and KCNA4 (By similarity). Interacts with LRRC4 and LRRC4B (By similarity). Interacts with SYNGAP1…
Cell membrane, Postsynaptic density, Synapse, Cytoplasm, Cell projection, axon, Cell projection, dendritic spine, Cell projection, dendrite, Presynapse
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5HEY | X-ray | 1.5 Å | A=302-402 |
| 5MZ7 | X-ray | 1.53 Å | A/B/C/D=303-402 |
| 1TP5 | X-ray | 1.54 Å | A=302-402 |
| 5HFD | X-ray | 1.6 Å | A=302-402 |
| 5HFB | X-ray | 1.62 Å | A=302-402 |
| 5HEB | X-ray | 1.65 Å | A=302-402 |
| 5HED | X-ray | 1.7 Å | A=302-402 |
| 5HF1 | X-ray | 1.75 Å | A=302-402 |
| 5HF4 | X-ray | 1.75 Å | A=302-402 |
| 5HFF | X-ray | 1.75 Å | A=302-402 |
| 1KJW | X-ray | 1.8 Å | A=430-724 |
| 5HDY | X-ray | 1.8 Å | A=302-402 |
| 5HFE | X-ray | 1.8 Å | A=302-402 |
| 7CQF | X-ray | 1.8 Å | A=309-422 |
| 1BE9 | X-ray | 1.82 Å | A=298-420 |
| 5HFC | X-ray | 1.85 Å | A=302-402 |
| 1TQ3 | X-ray | 1.89 Å | A=302-402 |
| 9IUI | X-ray | 1.93 Å | A/C=531-713 |
| 1TP3 | X-ray | 1.99 Å | A=302-402 |
| 1JXM | X-ray | 2.0 Å | A=430-724 |
Showing 20 of 42 experimental structures (best resolution first).
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