4FCR

Targeting conserved water molecules: Design of 4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine Hsp90 inhibitors using fragment-based screening and structure-based optimization

Summary for 4FCR

Related4FCP 4FCQ
DescriptorHeat shock protein HSP 90-alpha, 2-{[4-(2-chloro-4,5-dimethoxyphenyl)-5-cyano-7H-pyrrolo[2,3-d]pyrimidin-2-yl]sulfanyl}-N,N-dimethylacetamide (3 entities in total)
Functional Keywordsheat shock protein, hsp90, atpase, fragments, structure-based design, chaperone-chaperone inhibitor complex, chaperone/chaperone inhibitor
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm P07900
Total number of polymer chains1
Total molecular weight27033.67
Authors
Primary citation
Davies, N.G.,Browne, H.,Davis, B.,Drysdale, M.J.,Foloppe, N.,Geoffrey, S.,Gibbons, B.,Hart, T.,Hubbard, R.,Jensen, M.R.,Mansell, H.,Massey, A.,Matassova, N.,Moore, J.D.,Murray, J.,Pratt, R.,Ray, S.,Robertson, A.,Roughley, S.D.,Schoepfer, J.,Scriven, K.,Simmonite, H.,Stokes, S.,Surgenor, A.,Webb, P.,Wood, M.,Wright, L.,Brough, P.
Targeting conserved water molecules: Design of 4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine Hsp90 inhibitors using fragment-based screening and structure-based optimization.
Bioorg.Med.Chem., 20:6770-6789, 2012
PubMed: 23018093 (PDB entries with the same primary citation)
DOI: 10.1016/j.bmc.2012.08.050
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.698 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.24240.5%2.8%4.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
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PDB entries from 2020-08-05