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Yorodumi- PDB-3dep: Structural basis for specific substrate recognition by the chloro... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3dep | ||||||
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Title | Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43 | ||||||
Components |
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Keywords | PROTEIN TRANSPORT / MEMBRANE PROTEIN / Chloroplast SRP system / Signal recognition particle / signal sequence / ankyrin repeat / chromodomain / type I turn / substrate protein recognition / L18 region / LHCP / ANK repeat / Chloroplast / Coiled coil / Plastid / Ribonucleoprotein | ||||||
Function / homology | Function and homology information protein import into chloroplast thylakoid membrane / protein heterotrimerization / response to high light intensity / signal recognition particle, endoplasmic reticulum targeting / chloroplast envelope / chloroplast stroma / chloroplast thylakoid membrane / chloroplast / disordered domain specific binding / protein-macromolecule adaptor activity ...protein import into chloroplast thylakoid membrane / protein heterotrimerization / response to high light intensity / signal recognition particle, endoplasmic reticulum targeting / chloroplast envelope / chloroplast stroma / chloroplast thylakoid membrane / chloroplast / disordered domain specific binding / protein-macromolecule adaptor activity / protein domain specific binding / protein-containing complex / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.7 Å | ||||||
Authors | Holdermann, I. / Stengel, K.F. / Wild, K. / Sinning, I. | ||||||
Citation | Journal: Science / Year: 2008 Title: Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43. Authors: Stengel, K.F. / Holdermann, I. / Cain, P. / Robinson, C. / Wild, K. / Sinning, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3dep.cif.gz | 50.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3dep.ent.gz | 35.4 KB | Display | PDB format |
PDBx/mmJSON format | 3dep.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/de/3dep ftp://data.pdbj.org/pub/pdb/validation_reports/de/3dep | HTTPS FTP |
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-Related structure data
Related structure data | 3deoSC S: Starting model for refinement C: citing same article (ref.) |
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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: 20042.545 Da / Num. of mol.: 1 / Fragment: residues 85-267 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: CAO, At2g47450, T30B22.25 / Production host: Escherichia coli (E. coli) / References: UniProt: O22265 |
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#2: Protein/peptide | Mass: 1193.307 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic peptide |
#3: Chemical | ChemComp-CL / |
#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: 3.3 Å3/Da / Density % sol: 62.72 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.931 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 10, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.931 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→35 Å / Num. all: 10129 / Num. obs: 8435 / % possible obs: 99.1 % / Redundancy: 6.5 % / Rmerge(I) obs: 0.103 / Rsym value: 0.103 / Net I/σ(I): 3.6 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.451 / Mean I/σ(I) obs: 3.6 / Num. measured all: 8065 / Num. unique all: 1193 / Rsym value: 0.451 / % possible all: 99.6 |
-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 ID 3DEO Resolution: 2.7→35 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.903 / SU B: 14.793 / SU ML: 0.298 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.591 / ESU R Free: 0.355 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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 mean: 67.743 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→35 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.77 Å / Total num. of bins used: 20
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