RNA-binding protein FUS (FUS) is a 526-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35637.
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The mean pLDDT of this model is 53.6 (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 | 9% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 68% |
What pLDDT means and how to read it
DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response (PubMed:27731383). Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (PubMed:21256132). Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing (PubMed:26124092). Also binds its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay (PubMed:24204307). Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous…
Self-oligomerizes (via N-terminal region) (PubMed:25453086). Oligomerization is essential for chromatin binding (PubMed:25453086). Component of nuclear riboprotein complexes. Interacts with ILF3, TDRD3 and SF1 (PubMed:9660765). Interacts through its C-terminus with SFRS13A (PubMed:9774382). Interacts with OTUB1 and SARNP. Interacts with LRSAM1 (PubMed:27615052). Interacts with SAFB1 in a…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6KJ3 | EM | 0.6 Å | A=37-42 |
| 6KJ1 | EM | 0.65 Å | A=37-42 |
| 6KJ4 | EM | 0.65 Å | A=37-42 |
| 6KJ2 | EM | 0.67 Å | A=37-42 |
| 5XSG | EM | 0.73 Å | A=37-42 |
| 6BWZ | X-ray | 1.1 Å | A=37-42 |
| 6BXV | X-ray | 1.1 Å | A=54-61 |
| 6BZP | EM | 1.1 Å | A/B=77-82 |
| 5XRR | X-ray | 1.5 Å | A=54-59 |
| 4FDD | X-ray | 2.3 Å | B=498-526 |
| 6XFM | EM | 2.62 Å | 1/2/3/4/5/6/7/8=111-214 |
| 7CYL | X-ray | 2.7 Å | B=476-526 |
| 5YVI | X-ray | 2.9 Å | B=456-526 |
| 7VQQ | EM | 2.9 Å | A/B/C=2-214 |
| 4FQ3 | X-ray | 3.0 Å | B=493-526 |
| 5YVH | X-ray | 3.15 Å | B=371-526 |
| 5YVG | X-ray | 4.05 Å | X/Y=1-526 |
| 2LA6 | NMR | A=282-370 | |
| 2LCW | NMR | A=278-385 | |
| 5W3N | NMR | A/B/C/D/E/F/G/H/I=2-214 |
Showing 20 of 23 experimental structures (best resolution first).
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