6HFM
Hsp90 co-chaperone Cns1 C-domain from Saccharomyces cerevisiae
Summary for 6HFM
Entry DOI | 10.2210/pdb6hfm/pdb |
Descriptor | Hsp70/Hsp90 co-chaperone CNS1, MAGNESIUM ION (3 entities in total) |
Functional Keywords | unique fold, wheel domain, hsp90 co-chaperone, chaperone |
Biological source | Saccharomyces cerevisiae (Baker's yeast) |
Total number of polymer chains | 2 |
Total formula weight | 38352.94 |
Authors | Huber, E.M.,Groll, M. (deposition date: 2018-08-21, release date: 2019-03-27, Last modification date: 2024-05-15) |
Primary citation | Schopf, F.H.,Huber, E.M.,Dodt, C.,Lopez, A.,Biebl, M.M.,Rutz, D.A.,Muhlhofer, M.,Richter, G.,Madl, T.,Sattler, M.,Groll, M.,Buchner, J. The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2. Mol.Cell, 74:73-87.e8, 2019 Cited by PubMed: 30876805DOI: 10.1016/j.molcel.2019.02.011 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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