Transforming protein RhoA (RHOA) is a 193-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61586.
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The mean pLDDT of this model is 93.6 (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 | 89% |
| 70 to 90 | Confident: backbone generally right | 5% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle (PubMed:23871831). Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers (PubMed:31570889, PubMed:8910519, PubMed:9121475). Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis (PubMed:12900402, PubMed:16236794). Plays an essential role in cleavage furrow…
Interacts with ARHGEF28 (By similarity). Interacts (via GTP-bound form) with RIPOR1 (via N-terminus); this interaction links RHOA to STK24 and STK26 kinases (PubMed:27807006). Interacts with RIPOR2 (via active GTP- or inactive GDP-bound forms) isoform 1 and isoform 2; these interactions are direct, block the loading of GTP to RHOA and decrease upon chemokine CCL19 stimulation in primary T…
Cell membrane, Cytoplasm, cytoskeleton, Cleavage furrow, Cytoplasm, cell cortex, Midbody, Cell projection, lamellipodium, Cell projection, dendrite, Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6V6U | X-ray | 1.16 Å | A=1-181 |
| 5C4M | X-ray | 1.3 Å | A=1-193 |
| 7G83 | X-ray | 1.31 Å | A=1-184 |
| 6V6M | X-ray | 1.39 Å | A=1-181 |
| 7G8T | X-ray | 1.39 Å | A=1-184 |
| 6BCB | X-ray | 1.4 Å | F=1-181 |
| 6V6V | X-ray | 1.4 Å | A=1-181 |
| 8BNT | X-ray | 1.4 Å | A=1-184 |
| 8FPW | X-ray | 1.4 Å | A=1-181 |
| 8GI6 | X-ray | 1.4 Å | A=1-193 |
| 7G82 | X-ray | 1.41 Å | A=1-184 |
| 5C2K | X-ray | 1.42 Å | A=1-193 |
| 7G8B | X-ray | 1.42 Å | A=1-184 |
| 7G8F | X-ray | 1.42 Å | A=1-184 |
| 9VNG | X-ray | 1.43 Å | A=1-181 |
| 7G8R | X-ray | 1.44 Å | A=1-184 |
| 6KX2 | X-ray | 1.45 Å | A=1-181 |
| 7G8V | X-ray | 1.45 Å | A=1-184 |
| 7G94 | X-ray | 1.47 Å | A=1-184 |
| 8FPX | X-ray | 1.47 Å | A=1-181 |
Showing 20 of 130 experimental structures (best resolution first).
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