Filamin-A (FLNA) is a 2647-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21333.
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The mean pLDDT of this model is 76.6 (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 | 10% |
| 70 to 90 | Confident: backbone generally right | 67% |
| 50 to 70 | Low: treat with caution | 18% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK…
Homodimer. Interacts with PDLIM2 (By similarity). Interacts with RFLNA and RFLNB (By similarity). Interacts with FCGR1A, FLNB, FURIN, HSPB7, INPPL1, KCND2, MYOT, MYOZ1, ARHGAP24, PSEN1, PSEN2 and ECSCR. Also interacts with various other binding partners in addition to filamentous actin. Interacts (via N-terminus) with MIS18BP1 (via N-terminus). Interacts (via N-terminus) with TAF1B. Interacts…
Cytoplasm, cell cortex, Cytoplasm, cytoskeleton, Perikaryon, Cell projection, growth cone, Cell projection, podosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3CNK | X-ray | 1.65 Å | A/B=2559-2647 |
| 4M9P | X-ray | 1.72 Å | A=478-766 |
| 7SC4 | X-ray | 1.85 Å | A/B=2236-2329 |
| 2W0P | X-ray | 1.9 Å | A/B=2236-2329 |
| 4P3W | X-ray | 2.0 Å | A/B/C/D/E/F=2152-2329 |
| 2BRQ | X-ray | 2.1 Å | A/B=2236-2329 |
| 2JF1 | X-ray | 2.2 Å | A=2236-2329 |
| 9LWX | X-ray | 2.29 Å | A/B/C/D=2236-2329 |
| 3HOC | X-ray | 2.3 Å | A/B=2-269 |
| 3HOP | X-ray | 2.3 Å | A/B=2-269 |
| 6EW1 | X-ray | 2.31 Å | A=478-766 |
| 2BP3 | X-ray | 2.32 Å | A/B=1862-1956 |
| 3RGH | X-ray | 2.44 Å | A/B=1158-1252 |
| 9LXG | X-ray | 2.46 Å | A=2236-2330 |
| 2J3S | X-ray | 2.5 Å | A/B=2045-2329 |
| 3HOR | X-ray | 2.7 Å | A/B=2-269 |
| 3ISW | X-ray | 2.8 Å | A/B=2236-2329 |
| 2WFN | X-ray | 3.2 Å | A/B=1-278 |
| 6D8C | EM | 3.54 Å | A/B/C/D/E=1-278 |
| 2AAV | NMR | A=1863-1956 |
Showing 20 of 26 experimental structures (best resolution first).
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