GTPase KRas (KRAS) is a 189-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01116.
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The mean pLDDT of this model is 91.5 (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 | 78% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Signal transducer in the Ras-MAPK signaling pathway that regulates cell proliferation and survival (PubMed:22711838, PubMed:23698361). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:20949621, PubMed:39809765). Activates MAPK1/MAPK3 resulting in phosphorylation and ultimately degradation of GJA1 (By similarity). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (PubMed:24623306). Recognized by LZTR1 that mediates its ubiquitination by a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex (PubMed:40934300)
Interacts with PHLPP (By similarity). Interacts (active GTP-bound form preferentially) with RGS14 (By similarity). Interacts (when farnesylated) with PDE6D; this promotes dissociation from the cell membrane (PubMed:23698361). Interacts with SOS1 (PubMed:22431598). Interacts (when farnesylated) with GPR31 (PubMed:28619714). Interacts with RAP1GDS1 (PubMed:20709748, PubMed:24415755). Interacts…
Cell membrane, Endomembrane system, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9IAY | X-ray | 0.95 Å | A=1-164 |
| 9IAW | X-ray | 1.0 Å | A=1-164 |
| 6P0Z | X-ray | 1.01 Å | A/B=2-169 |
| 8ONV | X-ray | 1.01 Å | A=1-164 |
| 9IB5 | X-ray | 1.01 Å | A=1-164 |
| 8AZZ | X-ray | 1.02 Å | A=1-164 |
| 4QL3 | X-ray | 1.04 Å | A=1-169 |
| 8AZX | X-ray | 1.04 Å | A=1-164 |
| 8B00 | X-ray | 1.04 Å | A=1-164 |
| 8TVK | X-ray | 1.04 Å | A=1-169 |
| 8AZV | X-ray | 1.05 Å | A=1-164 |
| 9IB4 | X-ray | 1.06 Å | A=1-164 |
| 9E3S | X-ray | 1.08 Å | A/B=1-169 |
| 8AZY | X-ray | 1.09 Å | A=1-169 |
| 8B78 | X-ray | 1.11 Å | A=1-164 |
| 9N44 | X-ray | 1.11 Å | A=1-169 |
| 8AFB | X-ray | 1.12 Å | A=1-164 |
| 8FMI | X-ray | 1.12 Å | A=1-169 |
| 4TQA | X-ray | 1.13 Å | A/B=1-167 |
| 9BG4 | X-ray | 1.14 Å | A/B=1-169 |
Showing 20 of 488 experimental structures (best resolution first).
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