Dynein light chain 1, cytoplasmic (DYNLL1) is a 89-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63167.
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The mean pLDDT of this model is 95.3 (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 | 94% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Component of dynein, a family of motor proteins essential for movement along microtubules (By similarity). Required for structural and functional integrity of cilia (By similarity). Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (By similarity). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). In addition to its role in…
Homodimer (PubMed:18084006, PubMed:18650427). Monomer; the monomeric form is incapable of binding to target proteins (PubMed:18084006, PubMed:18650427). The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary…
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Chromosome, Cytoplasm, cytoskeleton, Nucleus, Mitochondrion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9NZ7 | X-ray | 1.41 Å | A/B/C=1-89 |
| 6GZL | X-ray | 1.95 Å | A=1-89 |
| 6GZJ | X-ray | 1.98 Å | A=1-89 |
| 3ZKE | X-ray | 2.2 Å | A/C/E/G/I/K=1-89 |
| 7D35 | X-ray | 2.4 Å | A=1-89 |
| 1CMI | X-ray | 2.5 Å | A/B=5-89 |
| 3ZKF | X-ray | 2.6 Å | A/C/E/G/I/K=1-89 |
| 9BLY | EM | 3.5 Å | I/J=1-89 |
| 6SC2 | EM | 3.9 Å | I/J/K/L/M/N=1-89 |
| 8RGG | EM | 4.0 Å | I/J=1-89 |
| 9E28 | EM | 4.4 Å | d/i=1-89 |
| 6RLB | EM | 4.5 Å | I/J/K/L/M/N=1-89 |
| 9E12 | EM | 4.5 Å | I/J=1-89 |
| 9E13 | EM | 4.5 Å | I/J=1-89 |
| 9E14 | EM | 5.0 Å | I/J=1-89 |
| 9YNH | EM | 5.5 Å | I/J=1-89 |
| 9E23 | EM | 6.2 Å | d/i=1-89 |
| 8PR1 | EM | 8.2 Å | D/E=1-89 |
| 9YNE | EM | 8.46 Å | d/i=1-89 |
| 8PR0 | EM | 9.4 Å | E/F=1-89 |
Showing 20 of 21 experimental structures (best resolution first).
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