Ras-related protein Rap-1b (RAP1B) is a 184-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61224.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 92.3 (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 | 80% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function
Heterodimer with RAP1GAP (PubMed:18309292). Interacts with EPAC2 (PubMed:18660803). Interacts with SGSM1 (PubMed:17509819). Interacts with SGSM2 (PubMed:17509819). Interacts with SGSM3 (PubMed:17509819). Interacts with KRIT1 (PubMed:22577140). Interacts with RAP1GDS1 (PubMed:24415755)
Cell membrane, Cytoplasm, cytosol, Cell junction
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4HDO | X-ray | 1.67 Å | B=1-167 |
| 6OQ4 | X-ray | 1.75 Å | B=1-167 |
| 6OQ3 | X-ray | 1.85 Å | B=1-167 |
| 6UZK | X-ray | 1.92 Å | B=1-167 |
| 4DXA | X-ray | 1.95 Å | A=1-167 |
| 4HDQ | X-ray | 1.95 Å | B=1-167 |
| 8SU8 | X-ray | 2.01 Å | B=1-167 |
| 8T09 | X-ray | 2.15 Å | B=1-167 |
| 3CF6 | X-ray | 2.2 Å | R=1-167 |
| 8T7V | X-ray | 2.25 Å | B=1-167 |
| 7C7I | X-ray | 2.28 Å | A/B=1-167 |
| 7C7J | X-ray | 2.39 Å | A/B=1-167 |
| 4MH0 | X-ray | 2.4 Å | R=1-167 |
| 4MGY | X-ray | 2.6 Å | R=1-167 |
| 4MGK | X-ray | 2.7 Å | R=1-167 |
| 5KHO | X-ray | 2.78 Å | C/D=1-167 |
| 4MGI | X-ray | 2.8 Å | R=1-167 |
| 6KYK | X-ray | 2.82 Å | C/D/E/F=1-167 |
| 4MGZ | X-ray | 3.0 Å | R=1-167 |
| 6AXF | X-ray | 3.1 Å | B/D/F/H/J/L/N/P=1-167 |
Showing 20 of 23 experimental structures (best resolution first).
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