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; PubMed: 30876805; DOI: 10.1016/j.molcel.2019.02.011

Experimental method

X-RAY DIFFRACTION (1.55 Å)