SAGA-associated factor 29 (SGF29) is a 293-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96ES7.
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The mean pLDDT of this model is 91.8 (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 | 83% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes (PubMed:19103755, PubMed:20850016, PubMed:21685874, PubMed:26421618, PubMed:26578293). SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3) (PubMed:20850016, PubMed:21685874, PubMed:26421618, PubMed:26578293). In the SAGA-type complexes, SGF29 is required to recruit complexes to H3K4me (PubMed:20850016). Involved in the response to endoplasmic reticulum (ER) stress by recruiting the SAGA complex to H3K4me, thereby promoting histone H3 acetylation and cell survival (PubMed:23894581).…
Interacts with dimethylated and trimethylated 'Lys-4' of histone H3 (H3K4me2 and H3K4me3), with a preference for the trimethylated form (H3K4me3) (PubMed:21685874, PubMed:26578293). Component of some SAGA-type complexes (PubMed:20850016). Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (PubMed:19103755).…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3MEA | X-ray | 1.26 Å | A=129-291 |
| 3MEU | X-ray | 1.28 Å | A/B=115-293 |
| 3ME9 | X-ray | 1.37 Å | A/B=115-293 |
| 5C0M | X-ray | 1.6 Å | A/B=115-293 |
| 3LX7 | X-ray | 1.78 Å | A=135-293 |
| 3MEV | X-ray | 1.83 Å | A/B=115-293 |
| 3MEW | X-ray | 1.92 Å | A=129-287 |
| 3MET | X-ray | 2.0 Å | A/B=115-293 |
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