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Yorodumi- PDB-5a52: The crystal structure of Arabidopsis thaliana CAR1 in complex wit... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5a52 | ||||||
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Title | The crystal structure of Arabidopsis thaliana CAR1 in complex with one calcium ion | ||||||
Components | CALCIUM-DEPENDENT LIPID-BINDING DOMAIN-CONTAINING PROTEIN | ||||||
Keywords | LIPID BINDING PROTEIN / CALCIUM BINDING PROTEIN / C2 DOMAIN | ||||||
Function / homology | Function and homology information positive regulation of abscisic acid-activated signaling pathway / abscisic acid-activated signaling pathway / GTPase activator activity / phospholipid binding / positive regulation of GTPase activity / : / lipid binding / calcium ion binding / protein homodimerization activity / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | ARABIDOPSIS THALIANA (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | ||||||
Authors | Fernandez, D. / Marquez, J.A. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2016 Title: Calcium-Dependent Oligomerization of Car Proteins at Cell Membrane Modulates Aba Signaling. Authors: Diaz, M. / Sanchez-Barrena, M.J. / Gonzalez-Rubio, J.M. / Rodriguez, L. / Fernandez, D. / Antoni, R. / Yunta, C. / Belda-Palazon, B. / Gonzalez-Guzman, M. / Peirats-Llobet, M. / Menendez, M. ...Authors: Diaz, M. / Sanchez-Barrena, M.J. / Gonzalez-Rubio, J.M. / Rodriguez, L. / Fernandez, D. / Antoni, R. / Yunta, C. / Belda-Palazon, B. / Gonzalez-Guzman, M. / Peirats-Llobet, M. / Menendez, M. / Boskovic, J. / Marquez, J.A. / Rodriguez, P.L. / Albert, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5a52.cif.gz | 46.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5a52.ent.gz | 32.8 KB | Display | PDB format |
PDBx/mmJSON format | 5a52.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a5/5a52 ftp://data.pdbj.org/pub/pdb/validation_reports/a5/5a52 | HTTPS FTP |
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-Related structure data
Related structure data | 5a4xC 5a50C 5a51C 4v29S C: citing same article (ref.) 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: 18867.793 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q9FHP6 | ||||||
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#2: Chemical | #3: Chemical | ChemComp-GOL / | #4: Chemical | ChemComp-CA / | #5: 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: 2.38 Å3/Da / Density % sol: 48.26 % / Description: NONE |
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Crystal grow | Details: 0.5 M MGSO4, 0.5 M HEPES PH 7.0 AND 1.6 M LITHIUM SULFATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.98 |
Detector | Type: DECTRIS PIXEL / Detector: PIXEL |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→23.23 Å / Num. obs: 22034 / % possible obs: 99.4 % / Observed criterion σ(I): 0 / Redundancy: 5.9 % / Biso Wilson estimate: 21.35 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 20.79 |
Reflection shell | Resolution: 1.65→1.75 Å / Redundancy: 5.9 % / Rmerge(I) obs: 0.7 / Mean I/σ(I) obs: 3.1 / % possible all: 99.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4V29 Resolution: 1.65→23.231 Å / SU ML: 0.16 / σ(F): 1.36 / Phase error: 23.94 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.65→23.231 Å
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Refine LS restraints |
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LS refinement shell |
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