+Open data
-Basic information
Entry | Database: PDB / ID: 7n1r | ||||||
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Title | A novel and unique ATP hydrolysis to AMP by a human Hsp70 BiP | ||||||
Components | Endoplasmic reticulum chaperone BiP | ||||||
Keywords | CHAPERONE / protein-ligand complex | ||||||
Function / homology | Function and homology information regulation of protein folding in endoplasmic reticulum / regulation of ATF6-mediated unfolded protein response / regulation of PERK-mediated unfolded protein response / ATF6 (ATF6-alpha) activates chaperones / ATF6B (ATF6-beta) activates chaperones / cerebellum structural organization / maintenance of protein localization in endoplasmic reticulum / negative regulation of IRE1-mediated unfolded protein response / IRE1alpha activates chaperones / cerebellar Purkinje cell layer development ...regulation of protein folding in endoplasmic reticulum / regulation of ATF6-mediated unfolded protein response / regulation of PERK-mediated unfolded protein response / ATF6 (ATF6-alpha) activates chaperones / ATF6B (ATF6-beta) activates chaperones / cerebellum structural organization / maintenance of protein localization in endoplasmic reticulum / negative regulation of IRE1-mediated unfolded protein response / IRE1alpha activates chaperones / cerebellar Purkinje cell layer development / ATF6 (ATF6-alpha) activates chaperone genes / regulation of IRE1-mediated unfolded protein response / endoplasmic reticulum chaperone complex / PERK regulates gene expression / protein folding in endoplasmic reticulum / misfolded protein binding / post-translational protein targeting to membrane, translocation / ERAD pathway / ER overload response / non-chaperonin molecular chaperone ATPase / chaperone cofactor-dependent protein refolding / endoplasmic reticulum-Golgi intermediate compartment / Regulation of HSF1-mediated heat shock response / cellular response to glucose starvation / negative regulation of protein-containing complex assembly / : / endoplasmic reticulum unfolded protein response / protein folding chaperone / heat shock protein binding / substantia nigra development / cellular response to interleukin-4 / response to endoplasmic reticulum stress / positive regulation of protein ubiquitination / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ATP-dependent protein folding chaperone / negative regulation of transforming growth factor beta receptor signaling pathway / melanosome / unfolded protein binding / ribosome binding / Platelet degranulation / midbody / protein-folding chaperone binding / protein refolding / positive regulation of cell migration / cadherin binding / protein domain specific binding / endoplasmic reticulum lumen / focal adhesion / intracellular membrane-bounded organelle / ubiquitin protein ligase binding / calcium ion binding / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / cell surface / endoplasmic reticulum / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / protein-containing complex / mitochondrion / extracellular exosome / ATP binding / membrane / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.03 Å | ||||||
Model details | A crystal structure of BiP in the complex with AMP after the hydrolysis of ATP included in the ...A crystal structure of BiP in the complex with AMP after the hydrolysis of ATP included in the crystallization buffer by BiP. | ||||||
Authors | Yang, J. / Musayev, F. / Liu, Q. | ||||||
Funding support | United States, 1items
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Citation | Journal: Protein Sci. / Year: 2022 Title: A novel and unique ATP hydrolysis to AMP by a human Hsp70 Binding immunoglobin protein (BiP). Authors: Li, H. / Musayev, F.N. / Yang, J. / Su, J. / Liu, Q. / Wang, W. / Fang, X. / Zhou, L. / Liu, Q. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7n1r.cif.gz | 281.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7n1r.ent.gz | 221.9 KB | Display | PDB format |
PDBx/mmJSON format | 7n1r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n1/7n1r ftp://data.pdbj.org/pub/pdb/validation_reports/n1/7n1r | HTTPS FTP |
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-Related structure data
Related structure data | 6asyS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 67237.977 Da / Num. of mol.: 2 / Fragment: UNP residue 25-633 / Mutation: L3,4 modification (TASDNQP to VGG) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HSPA5, GRP78 / Plasmid: pET28 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P11021, non-chaperonin molecular chaperone ATPase |
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-Non-polymers , 7 types, 1101 molecules
#2: Chemical | ChemComp-GOL / #3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-PO4 / #5: Chemical | #6: Chemical | #7: Chemical | ChemComp-PEG / | #8: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.41 % |
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Crystal grow | Temperature: 293 K / Method: evaporation / pH: 4.5 Details: 18-22% PEG1000, 0.1 M phosphate citrate, pH 4.5, 0.2 M lithium sulfate, 2% w/v dioxane |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4C / Wavelength: 0.979 Å |
Detector | Type: ADSC QUANTUM 1 / Detector: CCD / Date: Nov 30, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 83507 / % possible obs: 97.2 % / Redundancy: 1.9 % / Biso Wilson estimate: 35.976 Å2 / CC1/2: 0.985 / R split: 0.067 / Rrim(I) all: 0.095 / Net I/σ(I): 16.4 |
Reflection shell | Resolution: 2→2.03 Å / Redundancy: 1.8 % / Mean I/σ(I) obs: 3 / Num. unique obs: 5328 / CC1/2: 0.76 / CC star: 0.929 / Rpim(I) all: 0.369 / Rrim(I) all: 0.519 / Χ2: 2.004 / % possible all: 84.11 |
-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 6ASY Resolution: 2.03→45.31 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.929 / SU B: 4.673 / SU ML: 0.125 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.189 / ESU R Free: 0.168 / 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: 198.85 Å2 / Biso mean: 31.885 Å2 / Biso min: 3.8 Å2
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Refinement step | Cycle: final / Resolution: 2.03→45.31 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.03→2.083 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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