Rho GDP-dissociation inhibitor 1 (ARHGDIA) is a 204-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P52565.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 90.3 (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 | 76% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by…
Monomer (By similarity). Interacts with FER (PubMed:21122136). Interacts with PLXNB3 (By similarity). Forms a heterodimer with RAC1 (PubMed:23434736). Interacts with RHOA, the affinity is increased by three orders of magnitude when RHOA is prenylated (PubMed:20400958, PubMed:20628200, PubMed:23434736, PubMed:26646181). Interacts with PSMD10; the interaction increases ARHGDIA association with…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1KMT | X-ray | 1.3 Å | A/B=67-204 |
| 1QVY | X-ray | 1.6 Å | A/B/C/D=67-204 |
| 2JHX | X-ray | 1.6 Å | A/B=67-202 |
| 2JHU | X-ray | 1.65 Å | A/B=67-202 |
| 2JHT | X-ray | 1.88 Å | A/B/C/D=67-202 |
| 2JHY | X-ray | 1.9 Å | A=67-202 |
| 2JHS | X-ray | 1.95 Å | A=67-202 |
| 1FSO | X-ray | 2.0 Å | A=67-204 |
| 2JHV | X-ray | 2.07 Å | A/B/C/D/E/F=67-202 |
| 2JI0 | X-ray | 2.1 Å | A=67-202 |
| 2JHZ | X-ray | 2.2 Å | A/B=67-202 |
| 2BXW | X-ray | 2.4 Å | A/B=67-204 |
| 1RHO | X-ray | 2.5 Å | A/B/C=59-203 |
| 2JHW | X-ray | 2.5 Å | A/B=67-202 |
| 1FT0 | X-ray | 2.6 Å | A/B=67-204 |
| 1FST | X-ray | 2.7 Å | A/B=24-204 |
| 1HH4 | X-ray | 2.7 Å | D/E=1-204 |
| 1FT3 | X-ray | 2.8 Å | A/B=67-204 |
| 1CC0 | X-ray | 5.0 Å | E/F=1-204 |
| 2N80 | NMR | B=31-204 |
Showing 20 of 21 experimental structures (best resolution first).
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.