Cofilin-1 (CFL1) is a 166-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P23528.
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The mean pLDDT of this model is 87.6 (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 | 43% |
| 70 to 90 | Confident: backbone generally right | 53% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11812157, PubMed:33670794). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:15580268). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (PubMed:21834987). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake…
Can bind G- and F-actin in a 1:1 ratio of cofilin to actin (PubMed:11812157). It is a major component of intranuclear and cytoplasmic actin rods (By similarity). Interacts with the subcortical maternal complex (SCMC) via interaction with TLE6 isoform 1 and NLRP5 (By similarity). Interacts with C9orf72 (By similarity). Interacts with ABRACL; this interaction decreases CFL1-mediated actin…
Nucleus matrix, Cytoplasm, cytoskeleton, Cell projection, ruffle membrane, Cell projection, lamellipodium membrane, Cell projection, lamellipodium, Cell projection, growth cone, Cell projection, axon
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9H1F | X-ray | 1.8 Å | A=1-166 |
| 9QFJ | EM | 2.31 Å | F/G/H/I/J=1-166 |
| 5L6W | X-ray | 2.53 Å | C=1-166 |
| 9QFD | EM | 2.61 Å | H/I/J/K/L/M/N=1-166 |
| 9QFQ | EM | 2.76 Å | F/G/H/I/J=1-166 |
| 4BEX | X-ray | 2.8 Å | 1=1-166 |
| 9QFO | EM | 2.96 Å | G/H/I/J=1-166 |
| 9QFE | EM | 3.12 Å | H/I/J/K=1-166 |
| 9QFW | EM | 3.16 Å | F/G/H/I/J=1-166 |
| 6VAO | EM | 3.4 Å | F/G/H/I/J=1-166 |
| 9QFG | EM | 3.49 Å | H/I=1-166 |
| 5HVK | X-ray | 3.5 Å | B/D=2-166 |
| 9QFK | EM | 3.99 Å | J=1-166 |
| 6UBY | EM | 7.5 Å | I=1-166 |
| 6UC0 | EM | 7.5 Å | I=1-166 |
| 3J0S | EM | 9.0 Å | M/N/O/P/Q/R/S/T/U/V/W/X=1-166 |
| 6UC4 | EM | 9.2 Å | I/M/N/O/P=1-166 |
| 1Q8G | NMR | A=1-166 | |
| 1Q8X | NMR | A=1-166 |
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