Actin-related protein 2/3 complex subunit 2 (ARPC2) is a 300-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q3MHR7.
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The mean pLDDT of this model is 92.9 (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 | 83% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the mother actin filament. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand…
Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC (PubMed:11721045, PubMed:15505213). Interacts with SHANK3; the interaction probably mediates the association of SHANK3 with the Arp2/3 complex (By similarity). Interacts with DNAI3; this interaction reduces binding of the Arp2/3 complex to the VCA…
Cytoplasm, cytoskeleton, Cell projection, Synapse, synaptosome, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1K8K | X-ray | 2.0 Å | D=1-300 |
| 2P9I | X-ray | 2.46 Å | D=1-300 |
| 3UKR | X-ray | 2.48 Å | D=1-300 |
| 3ULE | X-ray | 2.5 Å | D=1-300 |
| 1TYQ | X-ray | 2.55 Å | D=1-300 |
| 1U2V | X-ray | 2.55 Å | D=1-300 |
| 2P9K | X-ray | 2.59 Å | D=1-300 |
| 2P9L | X-ray | 2.65 Å | D=1-300 |
| 3RSE | X-ray | 2.65 Å | D=1-300 |
| 2P9S | X-ray | 2.68 Å | D=1-300 |
| 3DXK | X-ray | 2.7 Å | D=1-300 |
| 2P9U | X-ray | 2.75 Å | D=1-300 |
| 3UKU | X-ray | 2.75 Å | D=1-300 |
| 2P9N | X-ray | 2.85 Å | D=1-300 |
| 3DXM | X-ray | 2.85 Å | D=1-300 |
| 8TAH | EM | 2.89 Å | D=1-300 |
| 2P9P | X-ray | 2.9 Å | D=1-300 |
| 9DLX | EM | 2.91 Å | D=1-285 |
| 9EAM | EM | 2.97 Å | D=1-300 |
| 4JD2 | X-ray | 3.08 Å | D=1-300 |
Showing 20 of 29 experimental structures (best resolution first).
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