6HFT
Hsp90 co-chaperone Cns1 from Saccharomyces cerevisiae (delta69)
Summary for 6HFT
| Entry DOI | 10.2210/pdb6hft/pdb |
| Related | 6HFM 6HFO |
| Descriptor | Hsp70/Hsp90 co-chaperone CNS1, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | hsp90 co-chaperone, two-domain fold, tpr domain, wheel domain, chaperone |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 36634.32 |
| Authors | Huber, E.M.,Groll, M. (deposition date: 2018-08-21, release date: 2019-03-27, Last modification date: 2024-01-17) |
| 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 (2.8 Å) |
Structure validation
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