Protein argonaute-2 (AGO2) is a 859-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UKV8.
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The mean pLDDT of this model is 92.4 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 85% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of…
Interacts with DICER1 through its Piwi domain and with TARBP2 during assembly of the RNA-induced silencing complex (RISC) (PubMed:14749716, PubMed:15973356, PubMed:16271387, PubMed:16289642, PubMed:16357216, PubMed:17507929, PubMed:18178619, PubMed:18690212, PubMed:33199684). Together, DICER1, AGO2 and TARBP2 constitute the trimeric RISC loading complex (RLC), or micro-RNA (miRNA) loading…
Cytoplasm, P-body, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9BF2 | X-ray | 1.59 Å | A/B/C=440-575 |
| 4Z4D | X-ray | 1.6 Å | A=1-859 |
| 3LUC | X-ray | 1.69 Å | A/B/C=439-575 |
| 3LUK | X-ray | 1.7 Å | A/B/C=439-575 |
| 7C6B | X-ray | 1.7 Å | A/B/C=440-578 |
| 9LSN | X-ray | 1.75 Å | A/B/C=440-574 |
| 9BF0 | X-ray | 1.78 Å | A/B/C=442-575 |
| 3LUJ | X-ray | 1.8 Å | A/B/C=439-575 |
| 4W5O | X-ray | 1.8 Å | A=1-859 |
| 4Z4E | X-ray | 1.8 Å | A=1-859 |
| 9LMZ | X-ray | 1.8 Å | A/B/C=440-574 |
| 3LUG | X-ray | 1.85 Å | A/B/C=439-575 |
| 6RA4 | X-ray | 1.9 Å | A/B=222-355 |
| 9BEZ | X-ray | 1.9 Å | A/B/C=440-575 |
| 3LUH | X-ray | 2.0 Å | A/B/C=439-575 |
| 3QX9 | X-ray | 2.0 Å | A/B/C=439-575 |
| 7D7U | X-ray | 2.0 Å | A/B/C=440-578 |
| 9OBD | X-ray | 2.02 Å | A=1-859 |
| 3LUD | X-ray | 2.1 Å | A/B/C=439-575 |
| 9LSO | X-ray | 2.13 Å | A/B/C=440-574 |
Showing 20 of 57 experimental structures (best resolution first).
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