Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PPARGC1A) is a 798-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UBK2.
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The mean pLDDT of this model is 52.8 (low 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 | 8% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 17% |
| Below 50 | Very low: often disordered regions | 62% |
What pLDDT means and how to read it
Transcriptional coactivator for steroid receptors and nuclear receptors (PubMed:10713165, PubMed:20005308, PubMed:21376232, PubMed:28363985, PubMed:32433991). Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter (PubMed:10713165, PubMed:20005308, PubMed:21376232). Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis (PubMed:10713165, PubMed:20005308, PubMed:21376232). Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism (PubMed:10713165,…
Homooligomer (PubMed:10713165). Interacts with MYBBP1A; inhibits MYBBP1A transcriptional activation (By similarity). Interacts with PRDM16, LPIN1 and PML (By similarity). Interacts (via LXXLL motif) with RORA and RORC (via AF-2 motif); activates RORA and RORC transcriptional activation (By similarity). Interacts with LRPPRC (PubMed:17050673). Interacts with FOXO1 (By similarity). Interacts with…
Nucleus, Nucleus, PML body, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9F7W | X-ray | 1.25 Å | B=136-154 |
| 8BF1 | X-ray | 1.36 Å | B=136-154 |
| 6MS7 | X-ray | 1.43 Å | B=141-151 |
| 6W9L | X-ray | 1.45 Å | B=141-152 |
| 9IWO | X-ray | 1.49 Å | B=137-151 |
| 3U9Q | X-ray | 1.52 Å | B=142-150 |
| 6NWL | X-ray | 1.59 Å | B=141-152 |
| 8YT9 | X-ray | 1.59 Å | B=135-156 |
| 9IWN | X-ray | 1.59 Å | B=137-151 |
| 3B1M | X-ray | 1.6 Å | B=136-154 |
| 3V9V | X-ray | 1.6 Å | C=136-154 |
| 6W9K | X-ray | 1.6 Å | B=142-151 |
| 9F7X | X-ray | 1.63 Å | B=136-154 |
| 3V9T | X-ray | 1.65 Å | C=136-154 |
| 6NWK | X-ray | 1.65 Å | B=141-152 |
| 5Q0I | X-ray | 1.7 Å | B=141-152 |
| 9T5S | X-ray | 1.74 Å | B/D=136-154 |
| 6IZN | X-ray | 1.75 Å | C=136-154 |
| 8YWU | X-ray | 1.77 Å | B=135-156 |
| 5Z5S | X-ray | 1.8 Å | C=136-154 |
Showing 20 of 47 experimental structures (best resolution first).
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