ADP-ribosylation factor-like protein 2 (ARL2) is a 184-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P36404.
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The mean pLDDT of this model is 94.3 (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 | 87% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear…
Found in a complex with ARL2, ARL2BP and SLC25A6 (PubMed:30945270). Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Found in a complex with ARL2, ARL2BP and SLC25A4. The GTP-bound form interacts with PDE6D. Interacts with ELMOD2. The GTP-bound form interacts with ARL2BP. Interacts, preferentially in its GDP-bound state, with TBCD (PubMed:10488091,…
Mitochondrion intermembrane space, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9M1J | EM | 2.14 Å | G=1-184 |
| 9M1M | EM | 2.21 Å | G=1-184 |
| 9M1N | EM | 2.24 Å | G=1-184 |
| 3DOE | X-ray | 2.25 Å | A=1-184 |
| 9M1K | EM | 2.45 Å | G=1-184 |
| 9M1I | EM | 2.48 Å | G=1-184 |
| 9M1L | EM | 2.55 Å | G=1-184 |
| 3DOF | X-ray | 3.3 Å | A=1-184 |
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