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Open data
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Basic information
Entry | Database: PDB / ID: 4hwi | ||||||
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Title | Crystal structure of ATBAG1 in complex with HSP70 | ||||||
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![]() | CHAPERONE/APOPTOSIS / BAG domain / ubiquitin-like domain / co-chaperone / complex with molecular chaperone / CHAPERONE-APOPTOSIS complex | ||||||
Function / homology | ![]() lumenal side of lysosomal membrane / regulation of protein import / negative regulation of supramolecular fiber organization / positive regulation of protein refolding / prostaglandin binding / positive regulation of lysosomal membrane permeability / lysosomal matrix / A1 adenosine receptor binding / cytoplasm protein quality control by the ubiquitin-proteasome system / protein carrier chaperone ...lumenal side of lysosomal membrane / regulation of protein import / negative regulation of supramolecular fiber organization / positive regulation of protein refolding / prostaglandin binding / positive regulation of lysosomal membrane permeability / lysosomal matrix / A1 adenosine receptor binding / cytoplasm protein quality control by the ubiquitin-proteasome system / protein carrier chaperone / response to nickel cation / clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane / Respiratory syncytial virus genome transcription / protein transmembrane import into intracellular organelle / Lipophagy / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / GABA synthesis, release, reuptake and degradation / protein targeting to lysosome involved in chaperone-mediated autophagy / late endosomal microautophagy / response to odorant / positive regulation by host of viral genome replication / synaptic vesicle uncoating / C3HC4-type RING finger domain binding / negative regulation of NLRP3 inflammasome complex assembly / clathrin coat disassembly / ATP-dependent protein disaggregase activity / CHL1 interactions / regulation of protein complex stability / photoreceptor ribbon synapse / maintenance of postsynaptic specialization structure / membrane organization / Prp19 complex / glycinergic synapse / presynaptic cytosol / postsynaptic specialization membrane / protein folding chaperone complex / positive regulation of mRNA splicing, via spliceosome / postsynaptic cytosol / regulation of postsynapse organization / negative regulation of cardiac muscle cell apoptotic process / Lysosome Vesicle Biogenesis / intermediate filament / chaperone-mediated autophagy / 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 / Regulation of HSF1-mediated heat shock response / regulation of protein-containing complex assembly / autophagosome / Attenuation phase / Protein methylation / ATP metabolic process / protein folding chaperone / skeletal muscle tissue development / positive regulation of phagocytosis / forebrain development / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / cellular response to cadmium ion / cellular response to starvation / photoreceptor inner segment / lysosomal lumen / mRNA Splicing - Major Pathway / cerebellum development / dendritic shaft / response to activity / kidney development / AUF1 (hnRNP D0) binds and destabilizes mRNA / response to progesterone / G protein-coupled receptor binding / ATP-dependent protein folding chaperone / peptide binding / spliceosomal complex / Late endosomal microautophagy / regulation of protein stability / PKR-mediated signaling / terminal bouton / ADP binding / mRNA splicing, via spliceosome / Chaperone Mediated Autophagy / cellular response to hydrogen peroxide / G1/S transition of mitotic cell cycle / positive regulation of T cell mediated cytotoxicity / protein import into nucleus / unfolded protein binding / melanosome / synaptic vesicle / late endosome / protein folding / response to estradiol / MHC class II protein complex binding / Clathrin-mediated endocytosis Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Shen, Y. / Fang, S. | ||||||
![]() | ![]() Title: Structural insight into plant programmed cell death mediated by BAG proteins in Arabidopsis thaliana. Authors: Fang, S. / Li, L. / Cui, B. / Men, S. / Shen, Y. / Yang, X. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 226 KB | Display | ![]() |
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PDB format | ![]() | 180 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 429.6 KB | Display | ![]() |
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Full document | ![]() | 433.3 KB | Display | |
Data in XML | ![]() | 21.3 KB | Display | |
Data in CIF | ![]() | 29.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4hwcSC ![]() 4hwdC ![]() 4hwfC ![]() 4hwhC ![]() 1hx1S S: Starting model for refinement C: citing same article ( |
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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: 41591.020 Da / Num. of mol.: 1 / Fragment: HSP70 ATPase domain (UNP residues 5-381) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 20185.732 Da / Num. of mol.: 1 / Fragment: BAG domain (UNP residues 66-242) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 54.29 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion / pH: 7.5 Details: 0.02 M citric acid / 0.08 M Bis-Tris propane, pH 8.8, 20% PEG3350, VAPOR DIFFUSION, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 5, 2011 | |||||||||
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 2.273→35.604 Å / Num. all: 30237 / Num. obs: 29495 / % possible obs: 99.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 | |||||||||
Reflection shell | Resolution: 2.273→2.34 Å / % possible all: 90.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 1HX1 AND 4HWC Resolution: 2.273→35.604 Å / SU ML: 0.33 / σ(F): 0 / Phase error: 27.62 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 28.363 Å2 / ksol: 0.376 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.273→35.604 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -3.9841 Å / Origin y: 11.2972 Å / Origin z: -12.5329 Å
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Refinement TLS group | Selection details: all |