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: 17382884 DOI: 10.1016/j.cell.2006.12.046 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation