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Yorodumi- PDB-1hx1: CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPAS... -
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-Basic information
Entry | Database: PDB / ID: 1hx1 | ||||||
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Title | CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN | ||||||
Components |
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Keywords | CHAPERONE/CHAPERONE INHIBITOR / PROTEIN-PROTEIN COMPLEX / APOPTOSIS / PROTEIN FOLDING / MOLECULAR CHAPERONE / NUCLEOTIDE EXCHANGE FACTOR / CHAPERONE-CHAPERONE INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information Regulation of HSF1-mediated heat shock response / Attenuation phase / HSF1-dependent transactivation / Protein methylation / GABA synthesis, release, reuptake and degradation / PKR-mediated signaling / mRNA Splicing - Major Pathway / synaptic vesicle uncoating / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / chaperone-mediated autophagy translocation complex disassembly ...Regulation of HSF1-mediated heat shock response / Attenuation phase / HSF1-dependent transactivation / Protein methylation / GABA synthesis, release, reuptake and degradation / PKR-mediated signaling / mRNA Splicing - Major Pathway / synaptic vesicle uncoating / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / adenyl-nucleotide exchange factor activity / protein targeting to lysosome involved in chaperone-mediated autophagy / late endosomal microautophagy / clathrin coat disassembly / AUF1 (hnRNP D0) binds and destabilizes mRNA / Clathrin-mediated endocytosis / Prp19 complex / presynaptic cytosol / Neutrophil degranulation / postsynaptic cytosol / non-chaperonin molecular chaperone ATPase / chaperone cofactor-dependent protein refolding / autophagosome / Regulation of HSF1-mediated heat shock response / protein folding chaperone / spliceosomal complex / heat shock protein binding / RNA splicing / ATP-dependent protein folding chaperone / terminal bouton / mRNA processing / melanosome / protein-macromolecule adaptor activity / protein-folding chaperone binding / protein refolding / lysosome / cell surface receptor signaling pathway / protein stabilization / ribonucleoprotein complex / lysosomal membrane / negative regulation of DNA-templated transcription / dendrite / apoptotic process / ubiquitin protein ligase binding / nucleolus / negative regulation of apoptotic process / ATP hydrolysis activity / nucleoplasm / ATP binding / membrane / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.9 Å | ||||||
Authors | Sondermann, H. / Scheufler, C. / Moarefi, I. | ||||||
Citation | Journal: Science / Year: 2001 Title: Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Authors: Sondermann, H. / Scheufler, C. / Schneider, C. / Hohfeld, J. / Hartl, F.U. / Moarefi, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hx1.cif.gz | 112.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hx1.ent.gz | 88.9 KB | Display | PDB format |
PDBx/mmJSON format | 1hx1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hx/1hx1 ftp://data.pdbj.org/pub/pdb/validation_reports/hx/1hx1 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 44509.086 Da / Num. of mol.: 1 / Fragment: ATPASE DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Gene: HSPA8, HSC70 / Production host: Escherichia coli (E. coli) / References: UniProt: P19120 |
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#2: Protein | Mass: 13157.168 Da / Num. of mol.: 1 / Fragment: BAG DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BAG1, HAP / Production host: Escherichia coli (E. coli) / References: UniProt: Q99933 |
#3: Chemical | ChemComp-TRS / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.11 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG3350, Tris, Na-K-tartrate, glycerol, DTT, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.5 | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.9→15 Å / Num. all: 43748 / Num. obs: 43748 / % possible obs: 99.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Biso Wilson estimate: 28.4 Å2 / Rmerge(I) obs: 0.056 / Net I/σ(I): 21 | ||||||||||||||||||
Reflection shell | Resolution: 1.9→2 Å / Rmerge(I) obs: 0.27 | ||||||||||||||||||
Reflection | *PLUS | ||||||||||||||||||
Reflection shell | *PLUS % possible obs: 99.6 % / Rmerge(I) obs: 0.27 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.9→14.9 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 1785682.69 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH and HUBER
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 64.29 Å2 / ksol: 0.371 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 49.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→14.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→2.02 Å / Rfactor Rfree error: 0.018 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 7.2 % / Rfactor obs: 0.234 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 49.8 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.399 / % reflection Rfree: 7.1 % / Rfactor Rwork: 0.351 |