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-Structure paper
| Title | NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90. |
|---|---|
| Journal, issue, pages | J. Biol. Chem., Vol. 294, Page 16010-16019, Year 2019 |
| Publish date | Apr 5, 2018 (structure data deposition date) |
Authors | Huck, J.D. / Que, N.L.S. / Immormino, R.M. / Shrestha, L. / Taldone, T. / Chiosis, G. / Gewirth, D.T. |
External links | J. Biol. Chem. / PubMed:31501246 |
| Methods | X-ray diffraction |
| Resolution | 1.49 - 2.3 Å |
| Structure data | ![]() PDB-6cyg: ![]() PDB-6cyh: ![]() PDB-6cyi: ![]() PDB-6d1x: |
| Chemicals | ![]() ChemComp-N5O: ![]() ChemComp-MG: ![]() ChemComp-HOH: ![]() ChemComp-N5A: ![]() ChemComp-PGE: ![]() ChemComp-PG4: ![]() ChemComp-PA7: |
| Source |
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Keywords | Chaperone/Inhibitor / HSP90 / Inhibitor / Chaperone / Chaperone-Inhibitor complex / GRP94 / Endoplasmic Reticulum / Co-crystal |
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homo sapiens (human)
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