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- PDB-7a4u: Crystal structure of lid-truncated apo BiP in an oligomeric state -
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Open data
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Basic information
Entry | Database: PDB / ID: 7a4u | ||||||
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Title | Crystal structure of lid-truncated apo BiP in an oligomeric state | ||||||
![]() | Endoplasmic reticulum chaperone BiP | ||||||
![]() | CHAPERONE / ER / Endoplasmic reticulum / Hsp70 / GRP78 | ||||||
Function / homology | ![]() negative regulation of IRE1-mediated unfolded protein response / endoplasmic reticulum chaperone complex / post-translational protein targeting to membrane, translocation / non-chaperonin molecular chaperone ATPase / negative regulation of protein-containing complex assembly / endoplasmic reticulum unfolded protein response / ATP-dependent protein folding chaperone / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / melanosome / endoplasmic reticulum lumen ...negative regulation of IRE1-mediated unfolded protein response / endoplasmic reticulum chaperone complex / post-translational protein targeting to membrane, translocation / non-chaperonin molecular chaperone ATPase / negative regulation of protein-containing complex assembly / endoplasmic reticulum unfolded protein response / ATP-dependent protein folding chaperone / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / melanosome / endoplasmic reticulum lumen / endoplasmic reticulum membrane / negative regulation of apoptotic process / perinuclear region of cytoplasm / cell surface / ATP hydrolysis activity / mitochondrion / ATP binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Perera, L.A. / Ron, D. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes. Authors: Preissler, S. / Rato, C. / Yan, Y. / Perera, L.A. / Czako, A. / Ron, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 126 KB | Display | ![]() |
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PDB format | ![]() | 94 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 432.2 KB | Display | ![]() |
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Full document | ![]() | 435.1 KB | Display | |
Data in XML | ![]() | 23.7 KB | Display | |
Data in CIF | ![]() | 35.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6zyhC ![]() 6zyiC ![]() 6zyjC ![]() 7a4vC ![]() 6habS 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 57543.043 Da / Num. of mol.: 1 / Mutation: T229A, V461F Source method: isolated from a genetically manipulated source Details: Ser27 is a remnant of an expression tag / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: G3I8R9, non-chaperonin molecular chaperone ATPase | ||||
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#2: Chemical | ChemComp-GOL / #3: Water | ChemComp-HOH / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.646473 Å3/Da / Density % sol: 53.55193 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1 M BIS-TRIS propane pH 7.5, 0.2 M trisodium citrate dihydrate, 20% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jul 30, 2020 |
Radiation | Monochromator: M / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.976 Å / Relative weight: 1 |
Reflection | Resolution: 1.77→58.92 Å / Num. obs: 58872 / % possible obs: 99.9 % / Redundancy: 3.2 % / CC1/2: 0.975 / Net I/σ(I): 9.9 |
Reflection shell | Resolution: 1.77→1.81 Å / Mean I/σ(I) obs: 1.1 / Num. unique obs: 3347 / CC1/2: 0.531 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6HAB Resolution: 1.77→58.91 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.953 / SU B: 3.381 / SU ML: 0.099 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.113 / ESU R Free: 0.11 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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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 max: 90 Å2 / Biso mean: 32.764 Å2 / Biso min: 17.28 Å2
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Refinement step | Cycle: final / Resolution: 1.77→58.91 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.77→1.816 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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