Endoribonuclease Dicer (DICER1) is a 1922-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UPY3.
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The mean pLDDT of this model is 67.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 16% |
| 70 to 90 | Confident: backbone generally right | 45% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 29% |
What pLDDT means and how to read it
Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also…
Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2; DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. Note that the trimeric RLC/miRLC is also referred to as RISC. Interacts with DHX9, AGO1, PIWIL1 and PRKRA. Associates with the 60S ribosome.…
Cytoplasm, Cytoplasm, perinuclear region
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4NGD | X-ray | 1.96 Å | A=765-1065 |
| 2EB1 | X-ray | 2.0 Å | A/B/C=1660-1852 |
| 4NGC | X-ray | 2.1 Å | A=765-1065 |
| 4NGB | X-ray | 2.25 Å | A=765-1065 |
| 4NH5 | X-ray | 2.55 Å | A=765-1065 |
| 4NH6 | X-ray | 2.55 Å | A=765-1065 |
| 4NGG | X-ray | 2.6 Å | A=765-1065 |
| 4NH3 | X-ray | 2.62 Å | A=765-1065 |
| 21CB | EM | 3.0 Å | A=26-1922 |
| 7XW2 | EM | 3.04 Å | A=1-1922 |
| 4NGF | X-ray | 3.1 Å | A/B/C/D=765-1065 |
| 4WYQ | X-ray | 3.2 Å | A/D=267-389 |
| 21CN | EM | 3.21 Å | D=26-1922 |
| 21CQ | EM | 3.29 Å | D=26-1922 |
| 9V43 | EM | 3.34 Å | B=26-1922 |
| 9V42 | EM | 3.37 Å | D=1-1922 |
| 4NHA | X-ray | 3.4 Å | A=765-1065 |
| 7XW3 | EM | 4.04 Å | A=1-1922 |
| 5ZAK | EM | 4.4 Å | A=1-1922 |
| 5ZAL | EM | 4.7 Å | A=1-1922 |
Showing 20 of 21 experimental structures (best resolution first).
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