Dynein light intermediate chain region of the dynein tail/dynactin/BICDR1 complex. Determined by electron microscopy at 3.4 Å resolution. Released 17 Jan 2018.
Explore 6F1Y in 3D Show helices and sheets RCSB PDB PDBe
6F1Y contains 21 α-helices and 9 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 781-796 | 16 | |
| α-helix | 801-821 | 21 | |
| α-helix | 830-862 | 33 | |
| α-helix | 871-890 | 20 | |
| α-helix | 896-925 | 30 | |
| α-helix | 973-1000 | 28 | |
| α-helix | 1001-1005 | 5 | |
| α-helix | 1036-1052 | 17 | |
| α-helix | 1076-1095 | 20 | |
| α-helix | 1111-1136 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-45 | 7 | |
| β-strand | 55-60 | 6 | 1 |
| α-helix | 67-74 | 8 | |
| β-strand | 89-93 | 5 | 1 |
| β-strand | 102-106 | 5 | 1 |
| β-strand | 108-109 | 2 | 1 |
| α-helix | 116-120 | 5 | |
| β-strand | 131-135 | 5 | 1 |
| α-helix | 142-163 | 22 | |
| α-helix | 169-181 | 13 | |
| β-strand | 227-230 | 4 | 1 |
| α-helix | 237-243 | 7 | |
| α-helix | 248-265 | 18 | |
| β-strand | 269-270 | 2 | 1 |
| α-helix | 280-288 | 9 | |
| β-strand | 301 | 1 | 1 |
| β-strand | 309-310 | 2 | 1 |
| α-helix | 319-323 | 5 | |
| α-helix | 336-339 | 4 | |
| α-helix | 362-370 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain | f | protein | 328 | Homo sapiens | Q14204 |
| Cytoplasmic dynein 1 light intermediate chain 2 | j | protein | 337 | Homo sapiens | O43237 (AlphaFold model) |
>6F1Y_1 Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain (chains f) SLIESVRTYERTCEKVEERNTISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAET VFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNRVQKAVDDLNLHSYSNLPIW VNKLDMEIERILGVRLQAGLRAWTQVLLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXLEESYSAVMGIVSEVEQYVKVXXXXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXXXXXXXXXX
>6F1Y_2 Cytoplasmic dynein 1 light intermediate chain 2 (chains j) SSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDE DRDDHTRCNVWILDGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVL REHIDKMKIPPEKMRELERKFVKDFQDYMEPEEGCQGSPQRRGPLTSGSDEENVALPLGD NVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAALIYTSVKE EKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAY EDFIVKPPVRKLVHDKELAAEDEQVFLMKQQSLLAKQ
Cryo-EM shows how dynactin recruits two dyneins for faster movement. Urnavicius, L., Lau, C.K., Elshenawy, M.M. et al. Nature (2018) 554:202-206. DOI 10.1038/nature25462 · PubMed
Other PDB entries of the same protein (UniProt Q14204), best resolution first:
MolViewer shows 6F1Y directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.