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- PDB-3jux: Structure of the translocation ATPase SecA from Thermotoga maritima -
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Open data
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Basic information
Entry | Database: PDB / ID: 3jux | ||||||
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Title | Structure of the translocation ATPase SecA from Thermotoga maritima | ||||||
![]() | Protein translocase subunit secA | ||||||
![]() | PROTEIN TRANSPORT / protein translocation / ATPase / conformational change / peptide binding / ATP-binding / Cell inner membrane / Cell membrane / Cytoplasm / Membrane / Nucleotide-binding / Translocation / Transport | ||||||
Function / homology | ![]() protein-exporting ATPase activity / cell envelope Sec protein transport complex / protein-secreting ATPase / protein transport by the Sec complex / intracellular protein transmembrane transport / protein import / protein targeting / ATP binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Zimmer, J. | ||||||
![]() | ![]() Title: Conformational flexibility and peptide interaction of the translocation ATPase SecA. Authors: Zimmer, J. / Rapoport, T.A. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 174.9 KB | Display | ![]() |
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PDB format | ![]() | 136.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 755.3 KB | Display | ![]() |
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Full document | ![]() | 800.4 KB | Display | |
Data in XML | ![]() | 34.9 KB | Display | |
Data in CIF | ![]() | 47.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3jv2C ![]() 1tf5S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Details | monomer |
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Components
#1: Protein | Mass: 94923.992 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-ADP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.83 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1M Hepes pH 7.5, 60% MPD, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 29, 2008 Details: double crystal monochromater with horizontal focusing sagittal bend second mono crystal with 4:1 magnification ratio and vertically focusing mirror. |
Radiation | Monochromator: double crystal monochromater / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.29 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→50 Å / Num. all: 19431 / Num. obs: 17570 / % possible obs: 99.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 6.8 % / Rsym value: 0.173 / Net I/σ(I): 13.6 |
Reflection shell | Resolution: 3.1→3.22 Å / Redundancy: 6.7 % / Mean I/σ(I) obs: 2.5 / Num. unique all: 1913 / Rsym value: 0.79 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1TF5 Resolution: 3.1→30 Å / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 1.5 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 42.3 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→30 Å
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LS refinement shell | Resolution: 3.1→3.13 Å /
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