|Entry||Database: PDB / ID: 1uyk|
|Title||Human Hsp90-alpha with 8-Benzo[1,3]dioxol-,5-ylmethyl-9-butyl-2-fluoro-9H-purin-6-ylamine|
|Components||HEAT SHOCK PROTEIN HSP 90-ALPHAHeat shock response|
|Keywords||CHAPERONE / HSP90 / ATPASE / PUX / ATP-BINDING / HEAT SHOCK|
|Function / homology|
Function and homology information
Signaling by ERBB2 / eNOS activation / Regulation of actin dynamics for phagocytic cup formation / HSP90 chaperone cycle for steroid hormone receptors (SHR) / vRNP Assembly / HSF1 activation / Sema3A PAK dependent Axon repulsion / Recruitment of NuMA to mitotic centrosomes / VEGFR2 mediated vascular permeability / Loss of proteins required for interphase microtubule organization from the centrosome ...Signaling by ERBB2 / eNOS activation / Regulation of actin dynamics for phagocytic cup formation / HSP90 chaperone cycle for steroid hormone receptors (SHR) / vRNP Assembly / HSF1 activation / Sema3A PAK dependent Axon repulsion / Recruitment of NuMA to mitotic centrosomes / VEGFR2 mediated vascular permeability / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Attenuation phase / VEGFA-VEGFR2 Pathway / Uptake and function of diphtheria toxin / HSF1-dependent transactivation / Interleukin-4 and Interleukin-13 signaling / Chaperone Mediated Autophagy / Estrogen-dependent gene expression / Extra-nuclear estrogen signaling / ESR-mediated signaling / Downregulation of ERBB2 signaling / AURKA Activation by TPX2 / The role of GTSE1 in G2/M progression after G2 checkpoint / Neutrophil degranulation / Constitutive Signaling by EGFRvIII / Regulation of PLK1 Activity at G2/M Transition / Scavenging by Class F Receptors / Anchoring of the basal body to the plasma membrane / PIWI-interacting RNA (piRNA) biogenesis / Loss of Nlp from mitotic centrosomes / positive regulation of protein polymerization / protein insertion into mitochondrial outer membrane / telomerase holoenzyme complex assembly / mitochondrial transport / chaperone-mediated autophagy / positive regulation of cellular protein catabolic process / central nervous system neuron axonogenesis / TPR domain binding / dendritic growth cone / chaperone-mediated protein complex assembly / telomere maintenance via telomerase / protein unfolding / axon extension / regulation of protein ubiquitination / DNA polymerase binding / regulation of protein complex assembly / regulation of cellular protein localization / cofactor metabolic process / positive regulation of tau-protein kinase activity / MHC class II protein complex binding / GTPase binding / protein tyrosine kinase binding / axonal growth cone / endocytic vesicle lumen / establishment of cell polarity / ciliary basal body-plasma membrane docking / response to unfolded protein / protein folding chaperone / regulation of nitric-oxide synthase activity / response to cold / positive regulation of telomerase activity / ATPase activity, coupled / lysosomal lumen / nitric-oxide synthase regulator activity / ERBB2 signaling pathway / tau protein binding / regulation of cellular response to heat / melanosome / histone deacetylase binding / vascular endothelial growth factor receptor signaling pathway / receptor-mediated endocytosis / regulation of G2/M transition of mitotic cell cycle / Fc-gamma receptor signaling pathway involved in phagocytosis / protein refolding / scaffold protein binding / unfolded protein binding / positive regulation of nitric oxide biosynthetic process / disordered domain specific binding / response to heat / myelin sheath / positive regulation of peptidyl-serine phosphorylation / G2/M transition of mitotic cell cycle / cellular response to heat / protein folding / protein stabilization / secretory granule lumen / ficolin-1-rich granule lumen / ATPase activity / positive regulation of protein phosphorylation / positive regulation of protein kinase B signaling / response to antibiotic / cytokine-mediated signaling pathway / neuronal cell body / ubiquitin protein ligase binding / nucleotide binding / neutrophil degranulation / perinuclear region of cytoplasm / signal transduction
Heat shock protein Hsp90, N-terminal / Ribosomal protein S5 domain 2-type fold / Heat shock protein Hsp90, conserved site / Histidine kinase/HSP90-like ATPase / Heat shock protein Hsp90 family / Histidine kinase/HSP90-like ATPase superfamily / Heat shock hsp90 proteins family signature. / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Hsp90 protein / HSP90, C-terminal domain
Heat shock protein HSP 90-alpha
|Biological species||HOMO SAPIENS (human)|
|Method||X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å|
|Authors||Wright, L. / Barril, X. / Dymock, B. / Sheridan, L. / Surgenor, A. / Beswick, M. / Drysdale, M. / Collier, A. / Massey, A. / Davies, N. / Fink, A. / Fromont, C. / Aherne, W. / Boxall, K. / Sharp, S. / Workman, P. / Hubbard, R.E.|
|Citation||Journal: Chem.Biol. / Year: 2004|
Title: Structure-Activity Relationships in Purine-Based Inhibitor Binding to Hsp90 Isoforms
Authors: Wright, L. / Barril, X. / Dymock, B. / Sheridan, L. / Surgenor, A. / Beswick, M. / Drysdale, M. / Collier, A. / Massey, A. / Davies, N. / Fink, A. / Fromont, C. / Aherne, W. / Boxall, K. / Sharp, S. / Workman, P. / Hubbard, R.E.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: HEAT SHOCK PROTEIN HSP 90-ALPHA
|#1: Protein/peptide|| |
Mass: 26601.773 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1-235
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: MELANOMA / Description: CLONED FROM IMAGE\:4026275 / Organ: SKIN / Plasmid: PET19 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P07900
|#2: Chemical|| ChemComp-PUX / |
|#3: Water|| ChemComp-HOH / |
|Compound details||MOLECULAR CHAPERONE HAS ATPASE ACTIVITY|
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.7 Å3/Da / Density % sol: 54 %|
|Crystal grow||pH: 6.5 |
Details: 25% PEG MME 2000, 0.1M NA CACODYLATE, PH6.5, 0.2M MGCL2., pH 6.50
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418|
|Detector||Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jan 15, 2003 / Details: OSMIC BLUE MIRRORS|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.5418 Å / Relative weight: 1|
|Reflection||Resolution: 2.6→30 Å / Num. obs: 9549 / % possible obs: 95.9 % / Redundancy: 1.39 % / Rmerge(I) obs: 0.073 / Net I/σ(I): 7|
|Reflection shell||Resolution: 2.6→2.7 Å / Redundancy: 1.35 % / Rmerge(I) obs: 0.291 / Mean I/σ(I) obs: 2 / % possible all: 88.4|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: PDB ENTRY 1YER
Resolution: 2.2→67.42 Å / SU B: 3.098 / SU ML: 0.088 / Cross valid method: THROUGHOUT / ESU R: 0.154 / ESU R Free: 0.141
Details: RESIDUE GLU A223 WAS THE LAST RESIDUE THAT WAS VISIBLE IN ELECTRON DENSITY.
|Displacement parameters||Biso mean: 28.336 Å2|
|Refinement step||Cycle: LAST / Resolution: 2.2→67.42 Å|
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