SERPINE1 mRNA-binding protein 1 (SERBP1) is a 408-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NC51.
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The mean pLDDT of this model is 54.2 (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 | 0% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 39% |
| Below 50 | Very low: often disordered regions | 47% |
What pLDDT means and how to read it
Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (PubMed:36691768). Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state (By similarity). May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay (PubMed:11001948). Seems to play a role in PML-nuclear bodies formation (PubMed:28695742)
Associates with mature 80S ribosomes (PubMed:23636399, PubMed:32687489, PubMed:36691768). Interacts with EEF2/eEF2; interaction sequesters EEF2/eEF2 at the A-site of the ribosome, thereby blocking the interaction sites of the mRNA-tRNA complex, promoting ribosome stabilization and hibernation (By similarity). Interacts with SPIN1 (By similarity). Interacts with CHD3 and TDRD3 (PubMed:12505151,…
Cytoplasm, Nucleus, Cytoplasm, perinuclear region
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9PBE | EM | 2.19 Å | CD=2-408 |
| 8K2C | EM | 2.4 Å | CB=1-408 |
| 8XSX | EM | 2.4 Å | CD=1-408 |
| 9P7D | EM | 2.57 Å | CD=1-408 |
| 9P7E | EM | 2.59 Å | CD=1-408 |
| 9PA7 | EM | 2.67 Å | CD=2-37 |
| 9P7C | EM | 2.78 Å | CD=1-408 |
| 9P7A | EM | 2.81 Å | CD=1-408 |
| 9B0P | EM | 2.82 Å | CD=183-241 |
| 9FQZ | EM | 2.85 Å | CD=1-408 |
| 6Z6N | EM | 2.9 Å | CD=1-408 |
| 9P78 | EM | 2.9 Å | CD=1-408 |
| 9RSX | EM | 2.91 Å | N3=1-408 |
| 9I2E | EM | 2.95 Å | CD=1-408 |
| 8XSY | EM | 3.0 Å | CB=1-408 |
| 8UKB | EM | 3.05 Å | CD=183-241 |
| 6Z6M | EM | 3.1 Å | CD=1-408 |
| 9P79 | EM | 3.1 Å | CD=1-408 |
| 9P8C | EM | 3.11 Å | CD=1-408 |
| 8XSZ | EM | 3.2 Å | CB=1-408 |
Showing 20 of 23 experimental structures (best resolution first).
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