5H22
Hsp90 alpha N-terminal domain in complex with an inhibitor
Summary for 5H22
| Entry DOI | 10.2210/pdb5h22/pdb |
| Descriptor | Hsp90aa1 protein, 4-chloranyl-7-[(4-methoxy-3,5-dimethyl-pyridin-2-yl)methyl]-5-(phenylmethyl)pyrrolo[2,3-d]pyrimidin-2-amine (3 entities in total) |
| Functional Keywords | hsp90, inhibitor, chaperone-inhibitor complex, chaperone/inhibitor |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 24517.17 |
| Authors | Kim, E.E.,Shin, S.C.,Keum, G.C. (deposition date: 2016-10-13, release date: 2017-10-11, Last modification date: 2023-11-08) |
| Primary citation | Lee, J.H.,Shin, S.C.,Seo, S.H.,Seo, Y.H.,Jeong, N.,Kim, C.W.,Kim, E.E.,Keum, G. Synthesis and in vitro antiproliferative activity of C5-benzyl substituted 2-amino-pyrrolo[2,3-d]pyrimidines as potent Hsp90 inhibitors. Bioorg. Med. Chem. Lett., 27:237-241, 2017 Cited by PubMed Abstract: A novel series of heat shock protein 90 (Hsp90) inhibitors was identified by X-ray crystal analysis of complex structures at solvent-exposed exit pocket C. The 2-amino-pyrrolo[2,3-d]pyrimidine derivatives, 7-deazapurines substituted with a benzyl moiety at C5, showed potent Hsp90 inhibition and broad-spectrum antiproliferative activity against NCI-60 cancer cell lines. The most potent compound, 6a, inhibited Hsp90 with an IC of 36nM and showed a submicromolar mean GI value against NCI-60 cell lines. The interaction of 6a at the ATP-binding pocket of Hsp90 was confirmed by X-ray crystallography and Western blot analysis. PubMed: 27914802DOI: 10.1016/j.bmcl.2016.11.062 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.499 Å) |
Structure validation
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