Growth factor receptor-bound protein 2 (GRB2) is a 217-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62993.
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The mean pLDDT of this model is 88.7 (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 | 68% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Non-enzymatic adapter protein that plays a pivotal role in precisely regulated signaling cascades from cell surface receptors to cellular responses, including signaling transduction and gene expression (PubMed:11016927, PubMed:11726515, PubMed:37626338). Thus, participates in many biological processes including regulation of innate and adaptive immunity, autophagy, DNA repair or necroptosis (PubMed:35831301, PubMed:37626338, PubMed:38182563). Controls signaling complexes at the T-cell antigen receptor to facilitate the activation, differentiation, and function of T-cells (PubMed:36864087, PubMed:9489702). Mechanistically, engagement of the TCR leads to phosphorylation of the adapter…
Homodimer (PubMed:36864087). Associates (via SH2 domain) with activated EGF and PDGF receptors (tyrosine phosphorylated) (PubMed:10026169, PubMed:19836242, PubMed:35831301). Interacts with PDGFRA (tyrosine phosphorylated); the interaction may be indirect (By similarity). Also associates to other cellular Tyr-phosphorylated proteins such as SIT1, IRS1, IRS2, IRS4, SHC and LNK; probably via the…
Nucleus, Cytoplasm, Endosome, Golgi apparatus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6ICG | X-ray | 1.15 Å | A/B=60-152 |
| 3WA4 | X-ray | 1.35 Å | A=60-152 |
| 1JYR | X-ray | 1.55 Å | A=60-151 |
| 2VWF | X-ray | 1.58 Å | A=158-214 |
| 2VVK | X-ray | 1.6 Å | A=161-214 |
| 3OV1 | X-ray | 1.6 Å | A=53-163 |
| 4P9V | X-ray | 1.64 Å | A=53-163 |
| 1GCQ | X-ray | 1.68 Å | A/B=159-217 |
| 2W0Z | X-ray | 1.7 Å | A=158-214 |
| 3C7I | X-ray | 1.7 Å | A=53-162 |
| 3IN8 | X-ray | 1.7 Å | A=53-163 |
| 3S8L | X-ray | 1.71 Å | A=53-163 |
| 3S8N | X-ray | 1.71 Å | A=53-163 |
| 1BMB | X-ray | 1.8 Å | A=49-168 |
| 1ZFP | X-ray | 1.8 Å | E=56-153 |
| 2AOB | X-ray | 1.8 Å | A/B/C/D=55-153 |
| 4P9Z | X-ray | 1.8 Å | A=53-163 |
| 6WM1 | X-ray | 1.8 Å | A/C=53-163 |
| 3OVE | X-ray | 1.82 Å | A=53-163 |
| 3S8O | X-ray | 1.85 Å | A=53-163 |
Showing 20 of 55 experimental structures (best resolution first).
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