NAD-dependent protein deacetylase sirtuin-3, mitochondrial (SIRT3) is a 399-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NTG7.
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The mean pLDDT of this model is 75.4 (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 | 59% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 29% |
What pLDDT means and how to read it
NAD-dependent protein deacetylase (PubMed:12186850, PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:19535340, PubMed:23283301, PubMed:24121500, PubMed:24252090). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed:12186850, PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:23283301, PubMed:24121500, PubMed:24252090, PubMed:38146092). Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA, MRPL12 and the ATP synthase subunit ATP5PO (PubMed:16788062, PubMed:18680753, PubMed:19535340, PubMed:24121500, PubMed:24252090, PubMed:38146092). Contributes to the regulation of the cellular…
Upon metabolic stress, forms a complex composed of FOXO3, SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301). Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (PubMed:29445193). Interacts with NDUFA9, ACSS1, IDH2 and GDH (PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:19535340). Interacts with…
Mitochondrion matrix
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8ANC | X-ray | 1.11 Å | P=98-108 |
| 4BN4 | X-ray | 1.3 Å | A=116-399 |
| 8V5U | X-ray | 1.48 Å | A=118-399 |
| 9S27 | X-ray | 1.6 Å | A=118-395 |
| 8CCW | X-ray | 1.65 Å | A=118-399 |
| 4JSR | X-ray | 1.7 Å | A=118-399 |
| 8V2N | X-ray | 1.74 Å | A=118-399 |
| 3GLR | X-ray | 1.8 Å | A=118-399 |
| 5D7N | X-ray | 1.83 Å | A/B/C/D/E/F=118-395 |
| 4BVH | X-ray | 1.9 Å | A/B/C=116-399 |
| 5Z94 | X-ray | 1.9 Å | A/B=117-399 |
| 5BWN | X-ray | 1.94 Å | A=118-399 |
| 5Z93 | X-ray | 1.95 Å | A=117-399 |
| 8CCZ | X-ray | 1.95 Å | A/B=118-399 |
| 9CBT | X-ray | 1.95 Å | A/B=118-399 |
| 4BV3 | X-ray | 2.0 Å | A=116-399 |
| 4BVB | X-ray | 2.0 Å | A=116-399 |
| 4C78 | X-ray | 2.0 Å | A=116-399 |
| 4O8Z | X-ray | 2.0 Å | A=116-399 |
| 8HLY | X-ray | 2.0 Å | A=119-399 |
Showing 20 of 44 experimental structures (best resolution first).
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