GTP-binding nuclear protein Ran (RAN) is a 216-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62826.
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The mean pLDDT of this model is 88.6 (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 | 69% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs (PubMed:10400640, PubMed:17209048, PubMed:26272610, PubMed:27306458, PubMed:8276887, PubMed:8636225, PubMed:8692944, PubMed:8896452, PubMed:9351834, PubMed:9428644, PubMed:9822603). Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis (PubMed:11336674, PubMed:26272610, PubMed:29040603, PubMed:7819259, PubMed:8636225, PubMed:8692944, PubMed:8896452, PubMed:9351834, PubMed:9428644, PubMed:9822603). Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and…
Monomer. Interacts with RANGAP1, which promotes RAN-mediated GTP hydrolysis (PubMed:7819259, PubMed:9428644). Interacts with KPNB1 (PubMed:10367892, PubMed:8896452, PubMed:9428644). Interaction with KPNB1 inhibits RANGAP1-mediated stimulation of GTPase activity (PubMed:9428644). Interacts with RCC1 which promotes the exchange of RAN-bound GDP by GTP (PubMed:11336674, PubMed:12194828,…
Nucleus, Nucleus envelope, Cytoplasm, cytosol, Cytoplasm, Melanosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3GJ0 | X-ray | 1.48 Å | A/B=2-216 |
| 7MO5 | X-ray | 1.55 Å | A=1-216 |
| 7MO1 | X-ray | 1.6 Å | A=1-216 |
| 5CIQ | X-ray | 1.65 Å | A/B=1-216 |
| 7MO2 | X-ray | 1.65 Å | A/C=1-216 |
| 5CIT | X-ray | 1.75 Å | A/B=1-216 |
| 5CIW | X-ray | 1.75 Å | A/B=1-216 |
| 5CJ2 | X-ray | 1.75 Å | A/B/C/D/E/F/G/H=1-216 |
| 1I2M | X-ray | 1.76 Å | A/C=1-216 |
| 4HAT | X-ray | 1.78 Å | A=1-216 |
| 3GJ3 | X-ray | 1.79 Å | A=2-216 |
| 3GJ5 | X-ray | 1.79 Å | A/C=2-216 |
| 4HB2 | X-ray | 1.8 Å | A=1-216 |
| 4WVF | X-ray | 1.8 Å | A=1-216 |
| 7CND | X-ray | 1.8 Å | A=1-216 |
| 7MNR | X-ray | 1.8 Å | A=1-216 |
| 7MNV | X-ray | 1.8 Å | A=1-216 |
| 3GJ8 | X-ray | 1.82 Å | A/C=2-216 |
| 4HAW | X-ray | 1.9 Å | A=1-216 |
| 4HAZ | X-ray | 1.9 Å | A=1-216 |
Showing 20 of 138 experimental structures (best resolution first).
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