GTPase NRas (NRAS) is a 189-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01111.
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The mean pLDDT of this model is 92.1 (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 | 12% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Signal transducer in the Ras-MAPK signaling pathway that regulates cell proliferation and survival (PubMed:30712867). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:30712867). Recognized by LZTR1 that mediates its ubiquitination by a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex (PubMed:40934300)
Interacts (active GTP-bound form preferentially) with RGS14 (By similarity). Interacts (active GTP-bound form) with RASSF7 (PubMed:21278800). Interacts (active GTP-bound form) with both SHOC2 and PP1c (all isoforms) to form a tertiary complex; SHOC2 and PP1c preferably bind M-Ras/MRAS, but they also bind K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS (PubMed:36175670, PubMed:35768504, PubMed:35831509,…
Cell membrane, Golgi apparatus membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9BG8 | X-ray | 1.2 Å | A/B=1-169 |
| 7F68 | X-ray | 1.24 Å | A=1-169 |
| 9BG3 | X-ray | 1.33 Å | A/B=1-169 |
| 6ZIO | X-ray | 1.55 Å | A/B=1-172 |
| 9Y3W | X-ray | 1.56 Å | A/B=1-169 |
| 8TBI | X-ray | 1.59 Å | A/B=1-172 |
| 9BG0 | X-ray | 1.64 Å | A/B=1-169 |
| 3CON | X-ray | 1.65 Å | A=1-172 |
| 6WGH | X-ray | 1.65 Å | A/B=1-170 |
| 5UHV | X-ray | 1.67 Å | A=1-166 |
| 9Y1Y | X-ray | 1.7 Å | A/B=1-169 |
| 9Y1X | X-ray | 1.72 Å | A/B=1-169 |
| 8VM2 | X-ray | 1.74 Å | A/B/C=1-172 |
| 9BGD | X-ray | 1.76 Å | A/B=1-169 |
| 6ZIZ | X-ray | 1.78 Å | A/B=1-172 |
| 9Y0G | X-ray | 1.8 Å | A/B=1-169 |
| 7OW4 | X-ray | 1.81 Å | C/F/I/L=7-16 |
| 9GLX | X-ray | 1.85 Å | A/B/C/D/E/F=1-169 |
| 6ULI | X-ray | 1.88 Å | C=10-18 |
| 6ULK | X-ray | 1.9 Å | C=10-19 |
Showing 20 of 35 experimental structures (best resolution first).
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