+Open data
-Basic information
Entry | Database: PDB / ID: 1fts | ||||||
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Title | SIGNAL RECOGNITION PARTICLE RECEPTOR FROM E. COLI | ||||||
Components | FTSY | ||||||
Keywords | SIGNAL RECOGNITION PARTICLE RECEPTOR / GTPASE / PROTEIN TARGETING | ||||||
Function / homology | Function and homology information signal recognition particle binding / signal-recognition-particle GTPase / SRP-dependent cotranslational protein targeting to membrane / stringent response / protein targeting / cytoplasmic side of plasma membrane / GTPase activity / GTP binding / protein homodimerization activity / ATP hydrolysis activity ...signal recognition particle binding / signal-recognition-particle GTPase / SRP-dependent cotranslational protein targeting to membrane / stringent response / protein targeting / cytoplasmic side of plasma membrane / GTPase activity / GTP binding / protein homodimerization activity / ATP hydrolysis activity / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 2.2 Å | ||||||
Authors | Montoya, G. / Svensson, C. / Luirink, J. / Sinning, I. | ||||||
Citation | Journal: Nature / Year: 1997 Title: Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Authors: Montoya, G. / Svensson, C. / Luirink, J. / Sinning, I. #1: Journal: Nature / Year: 1997 Title: Crystal Structure of the Ng Domain from the Signal-Recognition Particle Receptor Ftsy Authors: Montoya, G. / Svensson, C. / Luirink, J. / Sinning, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fts.cif.gz | 76.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fts.ent.gz | 57.9 KB | Display | PDB format |
PDBx/mmJSON format | 1fts.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fts_validation.pdf.gz | 358.9 KB | Display | wwPDB validaton report |
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Full document | 1fts_full_validation.pdf.gz | 363.5 KB | Display | |
Data in XML | 1fts_validation.xml.gz | 7.2 KB | Display | |
Data in CIF | 1fts_validation.cif.gz | 10.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ft/1fts ftp://data.pdbj.org/pub/pdb/validation_reports/ft/1fts | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 32182.012 Da / Num. of mol.: 1 / Fragment: NG-DOMAIN RESIDUES 197 - 497 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Cellular location: CYTOPLASM, CYTOPLASMA MEMBRANE / Plasmid: PET9 / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P10121 |
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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: 2.3 Å3/Da / Density % sol: 38 % | ||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion / pH: 6 / Details: VAPOR DIFFUSION, pH 6.0, vapor diffusion | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.99 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→30 Å / Num. obs: 15365 / % possible obs: 98 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Rsym value: 0.038 / Net I/σ(I): 15 |
Reflection | *PLUS Rmerge(I) obs: 0.038 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 2.2→7.5 Å / Cross valid method: YES / σ(F): 2
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Displacement parameters | Biso mean: 24 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→7.5 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.4 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |