14-3-3 protein zeta/delta (YWHAZ) is a 245-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63104.
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The mean pLDDT of this model is 93.9 (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 | 6% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 4% |
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:14578935, PubMed:15071501, PubMed:15644438, PubMed:16376338, PubMed:16959763, PubMed:31024343, PubMed:9360956). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:35662396). Binding generally results in the modulation of the activity of the binding partner (PubMed:35662396). Promotes cytosolic retention and inactivation of TFEB transcription factor by binding to phosphorylated TFEB (PubMed:35662396). Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (PubMed:16959763). In…
Interacts with CDK16 and BSPRY (By similarity). Interacts with WEE1 (C-terminal). Interacts with SAMSN1 (By similarity). Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm (By similarity). Interacts with Thr-phosphorylated ITGB2 (By similarity). Interacts with BCL2L11 (By similarity). Homodimer (PubMed:12865427, PubMed:16376338). Heterodimerizes with YWHAE…
Cytoplasm, Melanosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2O02 | X-ray | 1.5 Å | A/B=1-230 |
| 6F09 | X-ray | 1.59 Å | P/Q/R/S=1-230 |
| 7ZIT | X-ray | 1.79 Å | A/B=1-230 |
| 9UJ2 | X-ray | 1.8 Å | A/B=1-229 |
| 6ZFG | X-ray | 1.85 Å | A/B=1-229 |
| 6F08 | X-ray | 1.9 Å | A/B/I/J=1-230 |
| 6ZFD | X-ray | 1.9 Å | A/B=1-229 |
| 4FJ3 | X-ray | 1.95 Å | A/B=1-230 |
| 5EXA | X-ray | 1.95 Å | A/B=1-230 |
| 8P1H | X-ray | 1.95 Å | A/B=1-72, A/B=76-156, A/B=160-229 |
| 8A9G | X-ray | 1.96 Å | A/B=1-230 |
| 1QJA | X-ray | 2.0 Å | A/B=1-245 |
| 1QJB | X-ray | 2.0 Å | A/B=1-245 |
| 2C1N | X-ray | 2.0 Å | A/B=1-245 |
| 7D8P | X-ray | 2.0 Å | A/B=1-245 |
| 6YMO | X-ray | 2.02 Å | A/B=1-230 |
| 5NAS | X-ray | 2.08 Å | A/B=1-230 |
| 9FVL | X-ray | 2.08 Å | A/B=1-245 |
| 6YO8 | X-ray | 2.09 Å | A/B/C/D=1-230 |
| 5D2D | X-ray | 2.1 Å | A/B=1-230 |
Showing 20 of 77 experimental structures (best resolution first).
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