Ankyrin-3 (Ank3) is a 2622-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O70511.
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The mean pLDDT of this model is 57.3 (low 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 | 23% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 51% |
What pLDDT means and how to read it
Required for the organization of specialized membrane domains by linking the membrane to the cytoskeleton (By similarity). In neurons, participates in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (By similarity). In skeletal muscle, required for the localization of dystrophin (DMD) and beta-dystroglycan (betaDAG1) to costameres (By similarity). In rod photoreceptors, required for the transport of cyclic nucleotide-gated (CNG) channel subunits from the inner segment to the sensory cilium outer segment, which is critical for phototransduction and outer segment morphogenesis (By similarity). Regulates the activity of…
May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG. Directly interacts with DMD and betaDAG1; this interaction does not interfere with DMD-binding and is required for DMD and betaDAG1 retention at costameres. Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 7 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs)…
Cytoplasm, cytoskeleton, Cell projection, axon, Cell membrane, Cell membrane, sarcolemma, Postsynaptic cell membrane, Lysosome, Cell membrane, sarcolemma, T-tubule, Photoreceptor outer segment membrane, Cell projection, cilium membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5YIP | X-ray | 1.85 Å | B=1985-2010 |
| 6A9X | X-ray | 2.2 Å | A=1987-2010 |
| 7XCE | X-ray | 2.5 Å | A=275-500 |
| 5YIQ | X-ray | 2.6 Å | D=1985-2010 |
| 6M3P | X-ray | 3.31 Å | C/E=975-1465 |
| 6M3R | X-ray | 4.31 Å | E=975-1465 |
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