+Open data
-Basic information
Entry | Database: PDB / ID: 2fsh | ||||||
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Title | Complex SecA:AMP-PNP from Escherichia coli | ||||||
Components | Preprotein translocase secA subunit | ||||||
Keywords | PROTEIN TRANSPORT / ATPase / DNA-RNA helicase / Protein translocation / SecA | ||||||
Function / homology | Function and homology information preprotein binding / cell envelope Sec protein transport complex / protein-exporting ATPase activity / protein-secreting ATPase / protein transport by the Sec complex / intracellular protein transmembrane transport / protein import / protein targeting to membrane / protein secretion / protein targeting ...preprotein binding / cell envelope Sec protein transport complex / protein-exporting ATPase activity / protein-secreting ATPase / protein transport by the Sec complex / intracellular protein transmembrane transport / protein import / protein targeting to membrane / protein secretion / protein targeting / ribonucleoprotein complex binding / chaperone-mediated protein folding / cytoplasmic side of plasma membrane / ribosome binding / protein transport / zinc ion binding / ATP binding / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Papanikolau, Y. / Petratos, K. / Economou, A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structure of dimeric SecA, the Escherichia coli preprotein translocase motor. Authors: Papanikolau, Y. / Papadovasilaki, M. / Ravelli, R.B. / McCarthy, A.A. / Cusack, S. / Economou, A. / Petratos, K. #1: Journal: Febs Lett. / Year: 2005 Title: Escherichia coli SecA truncated at its termini is functional and dimeric Authors: Karamanou, S. / Sianidis, G. / Gouridis, G. / Pozidis, C. / Papanikolau, Y. / Papanikou, E. / Economou, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fsh.cif.gz | 305 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fsh.ent.gz | 240 KB | Display | PDB format |
PDBx/mmJSON format | 2fsh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fs/2fsh ftp://data.pdbj.org/pub/pdb/validation_reports/fs/2fsh | HTTPS FTP |
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-Related structure data
Related structure data | 2fsfC 2fsgSC 2fsiC 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: 97069.102 Da / Num. of mol.: 2 / Fragment: residues 9-861 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: secA, azi, pea, prlD / Plasmid: pET3a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21/pLysS / References: UniProt: P10408 #2: Chemical | #3: Water | ChemComp-HOH / | |
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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: 2.79 Å3/Da / Density % sol: 55.86 % |
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-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9762 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 3, 2003 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9762 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2→20 Å / Num. all: 143843 / Num. obs: 130193 / % possible obs: 90.5 % / Redundancy: 2.34 % / Biso Wilson estimate: 47.066 Å2 / Rmerge(I) obs: 0.051 / Net I/σ(I): 11.11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2FSG Resolution: 2→19.97 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.929 / SU B: 8.666 / SU ML: 0.124 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.168 / ESU R Free: 0.165 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 43.523 Å2
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Refinement step | Cycle: LAST / Resolution: 2→19.97 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.052 Å / Total num. of bins used: 20
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