2O0A
The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.
Summary for 2O0A
Entry DOI | 10.2210/pdb2o0a/pdb |
Descriptor | S.cerevisiae chromosome XVI reading frame ORF YPL253c, 1,2-ETHANEDIOL (3 entities in total) |
Functional Keywords | vik1, motor homology domain, kinesin, motor domain, microtubule-binding, kinesin-14, heterodimer, cell cycle-transport protein complex, cell cycle/transport protein |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Cellular location | Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body: Q12045 |
Total number of polymer chains | 1 |
Total formula weight | 34694.60 |
Authors | Allingham, J.S.,Sproul, L.R.,Rayment, I.,Gilbert, S.P. (deposition date: 2006-11-27, release date: 2007-03-27, Last modification date: 2023-12-27) |
Primary citation | Allingham, J.S.,Sproul, L.R.,Rayment, I.,Gilbert, S.P. Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site. Cell(Cambridge,Mass.), 128:1161-1172, 2007 Cited by PubMed: 17382884DOI: 10.1016/j.cell.2006.12.046 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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