The Structure of a Yeast Dynein Dyn2-Pac11 Complex and Effect on Single Molecule Dynein Motor Activity. Determined by X-ray diffraction at 1.9 Å resolution. Released 18 Sept 2013.
Explore 4HT6 in 3D Show helices and sheets RCSB PDB PDBe
4HT6 contains 6 α-helices and 16 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-16 | 7 | 1 |
| α-helix | 18-34 | 17 | |
| α-helix | 38-53 | 16 | |
| β-strand | 57-72 | 16 | 1 |
| β-strand | 75-81 | 7 | 1 |
| β-strand | 84-90 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 76-82 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-16 | 7 | 1 |
| α-helix | 18-32 | 15 | |
| α-helix | 38-53 | 16 | |
| β-strand | 57-72 | 16 | 1 |
| β-strand | 75-81 | 7 | 1 |
| β-strand | 84-90 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-16 | 7 | 2 |
| α-helix | 18-34 | 17 | |
| α-helix | 38-53 | 16 | |
| β-strand | 57-62 | 6 | 2 |
| β-strand | 66-72 | 7 | 3 |
| β-strand | 75-81 | 7 | 2 |
| β-strand | 84-90 | 7 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dynein light chain 1, cytoplasmic | A, C, E | protein | 97 | Saccharomyces cerevisiae | Q02647 (AlphaFold model) |
| WD repeat-containing protein PAC11 | B, D, F | protein | 11 | Saccharomyces cerevisiae | P40960 (AlphaFold model) |
>4HT6_1 Dynein light chain 1, cytoplasmic (chains A, C, E) GPLGSMSDENKSTPIVKASDITDKLKEDILTISKDALDKYQLERDIAGTVKKQLDVKYGN TWHVIVGKNFGSYVTHEKGHFVYFYIGPLAFLVFKTA
>4HT6_2 WD repeat-containing protein PAC11 (chains B, D, F) ITYDKGIQTDQ
The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization. Rao, L., Romes, E.M., Nicholas, M.P. et al. Mol Biol Cell (2013) 24:2362-2377. DOI 10.1091/mbc.E13-03-0166 · PubMed
Other PDB entries of the same protein (UniProt Q02647 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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