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Open data
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Basic information
Entry | Database: PDB / ID: 3fzf | ||||||
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Title | Crystal Structure of Hsc70/Bag1 in complex with ATP | ||||||
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![]() | CHAPERONE / HSP70 / HSC70 / BAG1 / heat shock / protein folding / adenosine / nucleoside / nucleotide exchange factor / small molecule inhibitor / ATP-binding / nucleotide-binding / stress response / apoptosis | ||||||
Function / homology | ![]() lumenal side of lysosomal membrane / regulation of protein import / protein transmembrane import into intracellular organelle / negative regulation of supramolecular fiber organization / positive regulation of protein refolding / prostaglandin binding / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / positive regulation of lysosomal membrane permeability ...lumenal side of lysosomal membrane / regulation of protein import / protein transmembrane import into intracellular organelle / negative regulation of supramolecular fiber organization / positive regulation of protein refolding / prostaglandin binding / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / positive regulation of lysosomal membrane permeability / lysosomal matrix / A1 adenosine receptor binding / late endosomal microautophagy / protein carrier chaperone / response to nickel cation / clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane / Respiratory syncytial virus genome transcription / Lipophagy / GABA synthesis, release, reuptake and degradation / protein targeting to lysosome involved in chaperone-mediated autophagy / adenyl-nucleotide exchange factor activity / response to odorant / positive regulation by host of viral genome replication / synaptic vesicle uncoating / C3HC4-type RING finger domain binding / positive regulation of smooth muscle cell apoptotic process / clathrin coat disassembly / negative regulation of NLRP3 inflammasome complex assembly / ATP-dependent protein disaggregase activity / CHL1 interactions / regulation of protein complex stability / photoreceptor ribbon synapse / maintenance of postsynaptic specialization structure / membrane organization / glycinergic synapse / Prp19 complex / presynaptic cytosol / protein folding chaperone complex / positive regulation of mRNA splicing, via spliceosome / postsynaptic specialization membrane / intermediate filament / regulation of postsynapse organization / negative regulation of cardiac muscle cell apoptotic process / Lysosome Vesicle Biogenesis / chaperone-mediated autophagy / postsynaptic cytosol / cellular response to steroid hormone stimulus / Golgi Associated Vesicle Biogenesis / phosphatidylserine binding / non-chaperonin molecular chaperone ATPase / positive regulation of proteolysis / chaperone cofactor-dependent protein refolding / HSF1-dependent transactivation / response to unfolded protein / estrous cycle / autophagosome / Regulation of HSF1-mediated heat shock response / regulation of protein-containing complex assembly / Attenuation phase / Protein methylation / ATP metabolic process / positive regulation of phagocytosis / skeletal muscle tissue development / forebrain development / protein folding chaperone / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / cellular response to cadmium ion / photoreceptor inner segment / cellular response to starvation / lysosomal lumen / mRNA Splicing - Major Pathway / cerebellum development / response to activity / dendritic shaft / kidney development / AUF1 (hnRNP D0) binds and destabilizes mRNA / response to progesterone / G protein-coupled receptor binding / ATP-dependent protein folding chaperone / spliceosomal complex / Late endosomal microautophagy / peptide binding / regulation of protein stability / PKR-mediated signaling / terminal bouton / ADP binding / mRNA splicing, via spliceosome / Chaperone Mediated Autophagy / cellular response to hydrogen peroxide / positive regulation of T cell mediated cytotoxicity / G1/S transition of mitotic cell cycle / protein import into nucleus / unfolded protein binding / melanosome / late endosome / protein folding / synaptic vesicle / response to estradiol / MHC class II protein complex binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Dokurno, P. / Williamson, D.S. / Murray, J.B. / Surgenor, A.E. | ||||||
![]() | ![]() Title: Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design Authors: Williamson, D.S. / Borgognoni, J. / Clay, A. / Daniels, Z. / Dokurno, P. / Drysdale, M.J. / Foloppe, N. / Francis, G.L. / Graham, C.J. / Howes, R. / Macias, A.T. / Murray, J.B. / Parsons, R. ...Authors: Williamson, D.S. / Borgognoni, J. / Clay, A. / Daniels, Z. / Dokurno, P. / Drysdale, M.J. / Foloppe, N. / Francis, G.L. / Graham, C.J. / Howes, R. / Macias, A.T. / Murray, J.B. / Parsons, R. / Shaw, T. / Surgenor, A.E. / Terry, L. / Wang, Y. / Wood, M. / Massey, A.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 116.2 KB | Display | ![]() |
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PDB format | ![]() | 87.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3fzhC ![]() 3fzkC ![]() 3fzlC ![]() 3fzmC ![]() 1hx1S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 42086.547 Da / Num. of mol.: 1 / Fragment: UNP residues 4-381 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 13157.168 Da / Num. of mol.: 1 / Fragment: UNP residues 222-334 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical | ChemComp-ATP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.03 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 15% PEG3350, 0.1M Tris buffer, 25mM sodium-potassium tartrate, pH8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Aug 14, 2006 / Details: mirrors |
Radiation | Monochromator: Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→24.87 Å / Num. all: 32145 / Num. obs: 32145 / % possible obs: 98.2 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 3.9 % / Rmerge(I) obs: 0.114 / Net I/σ(I): 3.3 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 3.96 % / Rmerge(I) obs: 0.539 / Mean I/σ(I) obs: 1.2 / % possible all: 97.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1HX1 Resolution: 2.2→24.87 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.906 / SU B: 10.215 / SU ML: 0.243 / Cross valid method: THROUGHOUT / σ(F): 1 / σ(I): 1 / ESU R: 0.382 / ESU R Free: 0.285 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.924 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→24.87 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.257 Å / Total num. of bins used: 20
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