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Yorodumi- PDB-7clt: Crystal structure of the EFhd1/Swiprosin-2, a mitochondrial actin... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7clt | ||||||
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Title | Crystal structure of the EFhd1/Swiprosin-2, a mitochondrial actin-binding protein | ||||||
Components | EF-hand domain-containing protein D1 | ||||||
Keywords | METAL BINDING PROTEIN / mitochondria / calcium-binding | ||||||
Function / homology | Function and homology information regulation of cellular hyperosmotic salinity response / calcium ion sensor activity / neuron projection development / mitochondrial inner membrane / calcium ion binding / mitochondrion Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.07380981063 Å | ||||||
Authors | Mun, S.A. / Park, J. / Park, K.R. / Lee, Y. / Kang, J.Y. / Park, T. / Jin, M. / Yang, J. / Jun, C.D. / Eom, S.H. | ||||||
Funding support | Korea, Republic Of, 1items
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Citation | Journal: Front Cell Dev Biol / Year: 2020 Title: Structural and Biochemical Characterization of EFhd1/Swiprosin-2, an Actin-Binding Protein in Mitochondria. Authors: Mun, S.A. / Park, J. / Park, K.R. / Lee, Y. / Kang, J.Y. / Park, T. / Jin, M. / Yang, J. / Jun, C.D. / Eom, S.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7clt.cif.gz | 43.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7clt.ent.gz | 23 KB | Display | PDB format |
PDBx/mmJSON format | 7clt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cl/7clt ftp://data.pdbj.org/pub/pdb/validation_reports/cl/7clt | HTTPS FTP |
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-Related structure data
Related structure data | 5i2lS 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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Unit cell |
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-Components
#1: Protein | Mass: 15192.491 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Efhd1, Sws2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9D4J1 | ||||||||
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#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.9 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 100 mM HEPES-NaOH, 5 mM ZnSO4, 25% (v/v) Jeffamine ED-2001 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 5C (4A) / Wavelength: 0.9794 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 30, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 2.07→50 Å / Num. obs: 8434 / % possible obs: 99.2 % / Redundancy: 4.9 % / Biso Wilson estimate: 24 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 2.07→2.11 Å / Rmerge(I) obs: 0.59 / Num. unique obs: 403 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5I2L Resolution: 2.07380981063→43.5995 Å / SU ML: 0.215981547602 / Cross valid method: FREE R-VALUE / σ(F): 1.36030208239 / Phase error: 22.4306799448 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.6235678918 Å2 | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.07380981063→43.5995 Å
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Refine LS restraints |
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LS refinement shell |
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