Cofilin-2 (CFL2) is a 166-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y281.
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The mean pLDDT of this model is 88.4 (confident 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 | 50% |
| 70 to 90 | Confident: backbone generally right | 46% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3 (PubMed:19752190). It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere (By similarity)
Interacts with CSRP3; possibly two molecules of CFL2 can interact with one molecule if CSRP3
Nucleus matrix, Cytoplasm, cytoskeleton
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9Y9P | EM | 2.06 Å | a/b/c/d/e=1-166 |
| 9Y9L | EM | 3.06 Å | a/b/c/d=1-166 |
| 9Y9M | EM | 3.06 Å | a/b/c=1-166 |
| 9Q7K | EM | 3.13 Å | a/b/c/d/e=1-166 |
| 9Y52 | EM | 3.46 Å | a/b/c/d/e=1-166 |
| 9Q7N | EM | 3.48 Å | a/b/c/d/e=1-166 |
| 9Q7M | EM | 3.5 Å | a/b/c/d=1-166 |
| 9Y9J | EM | 3.58 Å | a/b/c/d/e=1-166 |
| 9Q7L | EM | 3.68 Å | a/b/c=1-166 |
| 7M0G | NMR | A=1-166 | |
| 7U8K | NMR | K/L/M/N/O/P/Q/R=1-166 |
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