Small ribosomal subunit protein RACK1 (RACK1) is a 317-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63244.
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The mean pLDDT of this model is 92.4 (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 | 81% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6.…
Monomer; also forms homodimers and homooligomers (PubMed:15140893, PubMed:20529362). Interacts with CPNE3 (PubMed:20010870). May interact with ABCB4 (PubMed:19674157). Component of the small (40S) ribosomal subunit (PubMed:23636399). Interacts with the 80S ribosome (PubMed:23636399). Binds NHERF1. Forms a ternary complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1. Interacts with…
Cell membrane, Cytoplasm, Cytoplasm, perinuclear region, Nucleus, Perikaryon, Cell projection, dendrite, Cell projection, phagocytic cup
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8GLP | EM | 1.67 Å | Sg=1-317 |
| 8QOI | EM | 1.9 Å | Sg=1-317 |
| 9O3W | EM | 1.9 Å | Sg=1-317 |
| 8YOO | EM | 2.0 Å | Sg=1-317 |
| 9C3H | EM | 2.0 Å | Sg=1-317 |
| 7R4X | EM | 2.15 Å | g=1-317 |
| 9I2D | EM | 2.19 Å | Sg=1-317 |
| 9PBE | EM | 2.19 Å | Sg=2-314 |
| 8YOP | EM | 2.2 Å | Sg=1-317 |
| 9O3Y | EM | 2.2 Å | Sg=1-317 |
| 8JDK | EM | 2.26 Å | AR=1-317 |
| 8G5Y | EM | 2.29 Å | Sg=1-317 |
| 9S3D | EM | 2.32 Å | Sg=1-317 |
| 9RPV | EM | 2.35 Å | Rg/Sg=1-317 |
| 9S3B | EM | 2.38 Å | Sg=1-317 |
| 8K2C | EM | 2.4 Å | Sg=1-317 |
| 8XSX | EM | 2.4 Å | Sg=1-317 |
| 9SPF | EM | 2.4 Å | Sg=1-317 |
| 9SPI | EM | 2.4 Å | Sg=1-317 |
| 8JDL | EM | 2.42 Å | AR=1-317 |
Showing 20 of 178 experimental structures (best resolution first).
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