Cyclic GMP-AMP synthase (Cgas) is a 507-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8C6L5.
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The mean pLDDT of this model is 78.3 (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 | 58% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 28% |
What pLDDT means and how to read it
Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (PubMed:23258413, PubMed:23647843, PubMed:23722158, PubMed:26829768, PubMed:28214358, PubMed:29426904, PubMed:29625897, PubMed:32814054, PubMed:38740774). Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p] (PubMed:23258413, PubMed:23647843, PubMed:23722158, PubMed:26829768, PubMed:28214358). Acts as a key DNA sensor: directly binds double-stranded DNA (dsDNA), inducing the formation of liquid-like droplets in which…
Monomer in the absence of DNA (PubMed:28214358). Homodimer in presence of dsDNA: forms a 2:2 dimer with two enzymes binding to two DNA molecules (PubMed:28902841, PubMed:29426904). Interacts with nucleosomes; interaction is mainly mediated via histones H2A and H2B and inactivates the nucleotidyltransferase activity by blocking DNA-binding and subsequent activation (PubMed:32911480,…
Nucleus, Chromosome, Cell membrane, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8SHK | X-ray | 1.71 Å | C=147-507 |
| 8SHU | X-ray | 1.71 Å | C=147-507 |
| 8SHY | X-ray | 1.77 Å | C=147-507 |
| 5XZG | X-ray | 1.83 Å | A=147-507 |
| 4O6A | X-ray | 1.86 Å | A/B=147-507 |
| 4K98 | X-ray | 1.94 Å | A=147-507 |
| 4K99 | X-ray | 1.95 Å | A=147-507 |
| 4K8V | X-ray | 2.0 Å | A/B/C/D=147-507 |
| 7UTT | X-ray | 2.04 Å | A/C=147-507 |
| 4K96 | X-ray | 2.08 Å | A/B=147-507 |
| 5XZB | X-ray | 2.13 Å | A=149-505 |
| 7BUJ | X-ray | 2.13 Å | A/B=61-507 |
| 5XZE | X-ray | 2.18 Å | A=147-507 |
| 8SJ2 | X-ray | 2.23 Å | A/C=147-507 |
| 4K9A | X-ray | 2.26 Å | A=147-507 |
| 4K9B | X-ray | 2.26 Å | A=147-507 |
| 7UUX | X-ray | 2.26 Å | A/C=147-507 |
| 8G1J | X-ray | 2.3 Å | A/C=147-507 |
| 4LEZ | X-ray | 2.36 Å | A/C=142-507 |
| 8G2Q | X-ray | 2.37 Å | A/C=147-507 |
Showing 20 of 55 experimental structures (best resolution first).
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