6D1X
N-Domain Of Grp94, with the Charged Domain, In Complex With the Novel Ligand N-Propyl Carboxyamido Adenosine
Replaces: 1U0YSummary for 6D1X
Entry DOI | 10.2210/pdb6d1x/pdb |
Descriptor | Endoplasmin, N-PROPYL CARBOXYAMIDO ADENOSINE, TETRAETHYLENE GLYCOL, ... (4 entities in total) |
Functional Keywords | inhibitor, co-crystal, hsp90, chaperone |
Biological source | Canis lupus familiaris (Dog) |
Total number of polymer chains | 1 |
Total formula weight | 31960.79 |
Authors | Gewirth, D.T.,Immormino, R.M. (deposition date: 2018-04-12, release date: 2018-05-02, Last modification date: 2023-10-04) |
Primary citation | Huck, J.D.,Que, N.L.S.,Immormino, R.M.,Shrestha, L.,Taldone, T.,Chiosis, G.,Gewirth, D.T. NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90. J.Biol.Chem., 294:16010-16019, 2019 Cited by PubMed: 31501246DOI: 10.1074/jbc.RA119.009960 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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