RILP-like protein 2 (RILPL2) is a 211-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q969X0.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 77.2 (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 | 46% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 24% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). May function via activation of RAC1 and PAK1 (By similarity)
Homodimer (By similarity). Interacts with RAC1 (By similarity). Interacts (via N-terminus) with MYO5A, the interaction is required for its role in dendrite formation (By similarity). Interacts with RAB8A; interaction is dependent on the phosphorylation of RAB8A on 'Thr-72' (PubMed:29125462). Interacts with RAB10 and RAB12; interaction is dependent on the phosphorylation of 'Thr-73' on RAB10 and…
Cytoplasm, cytosol, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cell projection, cilium
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6SQ2 | X-ray | 1.68 Å | D/E=129-165 |
| 6RIR | X-ray | 1.77 Å | C/D=129-165 |
| 7LWB | X-ray | 1.9 Å | D=117-165 |
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.