Rho guanine nucleotide exchange factor 2 (ARHGEF2) is a 986-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92974.
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The mean pLDDT of this model is 69.2 (low 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 | 37% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 34% |
What pLDDT means and how to read it
Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent…
Found in a complex composed at least of ARHGEF2, NOD2 and RIPK2. Interacts with RIPK2; the interaction mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK. Interacts with RIPK1 and RIPK3. Interacts with YWHAZ/14-3-3 zeta; when phosphorylated at Ser-886. Interacts with the kinases PAK4, AURKA and MAPK1. Interacts with RHOA and RAC1. Interacts with NOD1. Interacts (via the N-terminal zinc…
Cytoplasm, cytoskeleton, Cytoplasm, Cell junction, tight junction, Golgi apparatus, Cytoplasm, cytoskeleton, spindle, Cell projection, ruffle membrane, Cytoplasmic vesicle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7G83 | X-ray | 1.31 Å | B=206-448 |
| 7G8T | X-ray | 1.39 Å | B=206-448 |
| 8BNT | X-ray | 1.4 Å | B=206-448 |
| 7G82 | X-ray | 1.41 Å | B=206-448 |
| 7G8B | X-ray | 1.42 Å | B=206-448 |
| 7G8F | X-ray | 1.42 Å | B=206-448 |
| 7G8R | X-ray | 1.44 Å | B=206-448 |
| 7G8V | X-ray | 1.45 Å | B=206-448 |
| 7G94 | X-ray | 1.47 Å | B=206-448 |
| 7G8K | X-ray | 1.49 Å | B=206-448 |
| 7G8A | X-ray | 1.5 Å | B=206-448 |
| 7G81 | X-ray | 1.51 Å | B=206-448 |
| 7G8Z | X-ray | 1.51 Å | B=206-448 |
| 7G95 | X-ray | 1.55 Å | B=206-448 |
| 7G8Q | X-ray | 1.56 Å | B=206-448 |
| 7G8O | X-ray | 1.58 Å | B=206-448 |
| 7G8L | X-ray | 1.6 Å | B=206-448 |
| 7G8S | X-ray | 1.6 Å | B=206-448 |
| 7G80 | X-ray | 1.67 Å | B=206-448 |
| 7G8H | X-ray | 1.67 Å | B=206-448 |
Showing 20 of 60 experimental structures (best resolution first).
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