Dynamin-1 (Dnm1) is a 864-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21575.
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The mean pLDDT of this model is 77.9 (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 | 37% |
| 70 to 90 | Confident: backbone generally right | 39% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission and participates in many forms of endocytosis, such as clathrin-mediated endocytosis or synaptic vesicle endocytosis as well as rapid endocytosis (RE). Associates to the membrane, through lipid binding, and self-assembles into rings and stacks of interconnected rings through oligomerization to form a helical polymer around the vesicle membrane leading to constriction of invaginated coated pits around their necks. Self-assembly of the helical polymer induces membrane tubules narrowing until the polymer reaches a length sufficient to trigger GTP hydrolysis. Depending on the curvature imposed on the tubules,…
Homodimer; homodimerization is mediated by the dynamin-type G domain which promotes assembly-stimulated GTPase activity. Homo-tetramer formed from two dimers in the absence of lipid. Oligomerizes into a helical polymer that self-assembles around the vesicle membrane, when associated to the membrane through lipid binding. Interacts (via C-terminal proline-rich domain (PRD)) with SNX9 (via SH3…
Cytoplasmic vesicle, clathrin-coated vesicle, Golgi apparatus, Cell membrane, Membrane, clathrin-coated pit, Cytoplasmic vesicle, Presynapse, Cytoplasmic vesicle, secretory vesicle, chromaffin granule
Compare the prediction with experimentally determined structures of the same protein:
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