14-3-3 protein gamma (YWHAG) is a 247-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61981.
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The mean pLDDT of this model is 94.2 (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 | 89% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:15696159, PubMed:16511572, PubMed:36732624). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:15696159, PubMed:16511572, PubMed:36732624). Binding generally results in the modulation of the activity of the binding partner (PubMed:16511572). Promotes inactivation of WDR24 component of the GATOR2 complex by binding to phosphorylated WDR24 (PubMed:36732624). Participates in the positive regulation of NMDA glutamate receptor activity by promoting the L-glutamate secretion through interaction with BEST1…
Homodimer (PubMed:17085597). Forms heterodimers with SFN, YWHAB or YWHAQ (By similarity). Part of a complex that contains DSG3, PKP1, YAP1 and YWHAG; the complex is required for localization of DSG3 and YAP1 to the cell membrane in keratinocytes (PubMed:31835537). Interacts with YAP1 (By similarity). Interacts with SAMSN1 (By similarity). Interacts with RAF1, SSH1 and CRTC2/TORC2…
Cytoplasm, cytosol, Mitochondrion matrix
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6S9K | X-ray | 1.6 Å | A=1-234 |
| 6ZBT | X-ray | 1.8 Å | A/B/C/D=1-234 |
| 3UZD | X-ray | 1.86 Å | A=1-247 |
| 6ZC9 | X-ray | 1.9 Å | A/B/C/D=1-234 |
| 6A5S | X-ray | 2.1 Å | A/B/D/G=1-247 |
| 4E2E | X-ray | 2.25 Å | A=1-247 |
| 7A6Y | X-ray | 2.5 Å | A/B/C/D=1-234 |
| 2B05 | X-ray | 2.55 Å | A/B/C/D/E/F=2-247 |
| 6GKF | X-ray | 2.6 Å | A/B/C/D/E/F/G/H=1-234 |
| 6BZD | X-ray | 2.67 Å | A/B/C/D=2-247 |
| 7A6R | X-ray | 2.7 Å | A/B/C/D=1-234 |
| 5D3E | X-ray | 2.75 Å | A/B/E/F/I/J=1-238 |
| 6SAD | X-ray | 2.75 Å | A/B=1-234 |
| 6FEL | X-ray | 2.84 Å | A/B/C/D=1-234 |
| 6GKG | X-ray | 2.85 Å | A/B/C/D/E/F/G/H=1-234 |
| 4O46 | X-ray | 2.9 Å | A/B/C/D/E/F=1-247 |
| 6BYJ | X-ray | 2.9 Å | A/B/C/D/E/F=2-241 |
| 6Y4K | X-ray | 3.0 Å | A/B=1-234 |
| 4J6S | X-ray | 3.08 Å | A/B/C/D=2-247 |
| 6Y6B | X-ray | 3.08 Å | A/B=1-234 |
Showing 20 of 22 experimental structures (best resolution first).
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