Ras GTPase-activating protein-binding protein 1 (G3BP1) is a 466-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13283.
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The mean pLDDT of this model is 66.8 (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 | 28% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 43% |
What pLDDT means and how to read it
Protein involved in various processes, such as stress granule formation and innate immunity (PubMed:37672657, PubMed:20180778, PubMed:23279204, PubMed:30510222, PubMed:30804210). Plays an essential role in stress granule formation (PubMed:37672657, PubMed:20180778, PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:35977029, PubMed:36183834, PubMed:36279435, PubMed:36692217, PubMed:37379838). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:37672657, PubMed:20180778, PubMed:23279204, PubMed:27022092, PubMed:32302570, PubMed:32302571,…
Homodimer and oligomer (PubMed:37672657, PubMed:24324649). Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP1 (By similarity). Binds to the SH3 domain of Ras GTPase-activating protein (RASA1) in proliferating cells (By similarity). No interaction in quiescent cells (By similarity). Interacts (via NTF2 domain) with USP10; inhibiting stress granule formation by…
Cytoplasm, cytosol, Perikaryon, Cytoplasm, Stress granule, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4FCJ | X-ray | 1.62 Å | A/B=1-139 |
| 3Q90 | X-ray | 1.7 Å | A/B=1-139 |
| 8TH1 | X-ray | 1.8 Å | A/B/C/D=1-139 |
| 5FW5 | X-ray | 1.92 Å | A/B=1-139 |
| 6TA7 | X-ray | 1.93 Å | A/B/C/D/E/F=1-139 |
| 8TH6 | X-ray | 2.34 Å | A/B/C/D=1-139 |
| 7SUO | X-ray | 2.35 Å | A/B=2-139 |
| 7S17 | X-ray | 2.36 Å | A/B=1-138 |
| 9CC6 | X-ray | 2.4 Å | B=453-465 |
| 7XHG | X-ray | 2.46 Å | A/B/C/D=1-139 |
| 8TH5 | X-ray | 2.62 Å | A/B/C/D/E/F/G/H/I/J=1-139 |
| 9IVQ | EM | 2.66 Å | A/B/C/D/E/F/G/H/M/N/O/P/Q/R/S/T=1-138 |
| 7XHF | X-ray | 2.68 Å | A/B=1-139 |
| 8V1L | X-ray | 2.68 Å | A/B/C/D/E/F=1-139 |
| 4FCM | X-ray | 2.69 Å | A/B=1-139 |
| 9IVR | EM | 2.8 Å | A/B/C/D/E/F/G/H/M/N/O/P/Q/R/S/T=1-138 |
| 9J5S | X-ray | 2.84 Å | A/B=1-138 |
| 8TH7 | X-ray | 2.88 Å | A/B=1-139 |
| 9IVS | EM | 2.97 Å | A/B/C/D/E/F/G/H/M/N/O/P/Q/R/S/T=1-138 |
| 4IIA | X-ray | 3.3 Å | A=11-139 |
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