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Open data
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Basic information
Entry | Database: PDB / ID: 5aww | ||||||
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Title | Precise Resting State of Thermus thermophilus SecYEG | ||||||
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![]() | PROTEIN TRANSPORT/IMMUNE SYSTEM / translocon / membrane protein / PROTEIN TRANSPORT-IMMUNE SYSTEM complex | ||||||
Function / homology | ![]() cell envelope Sec protein transport complex / protein transport by the Sec complex / intracellular protein transmembrane transport / protein-transporting ATPase activity / signal sequence binding / SRP-dependent cotranslational protein targeting to membrane, translocation / protein secretion / protein transmembrane transporter activity / protein targeting / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Tanaka, Y. / Sugano, Y. / Takemoto, M. / Kusakizako, T. / Kumazaki, K. / Ishitani, R. / Nureki, O. / Tsukazaki, T. | ||||||
![]() | ![]() Title: Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State. Authors: Tanaka, Y. / Sugano, Y. / Takemoto, M. / Mori, T. / Furukawa, A. / Kusakizako, T. / Kumazaki, K. / Kashima, A. / Ishitani, R. / Sugita, Y. / Nureki, O. / Tsukazaki, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 126.4 KB | Display | ![]() |
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PDB format | ![]() | 97.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 21.5 KB | Display | |
Data in CIF | ![]() | 28.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5ch4C ![]() 2zjsS C: citing same article ( S: Starting model for refinement |
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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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Components
#1: Protein | Mass: 48957.516 Da / Num. of mol.: 1 / Mutation: L2V, R252G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: HB8 / ATCC 27634 / DSM 579 / Gene: secY, TTHA1672 Production host: ![]() ![]() References: UniProt: Q5SHQ8 | ||
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#2: Protein | Mass: 7072.410 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: HB8 / ATCC 27634 / DSM 579 / Gene: secE, TTHA0249 Production host: ![]() ![]() References: UniProt: P38383 | ||
#3: Protein | Mass: 7943.501 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 43-116 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: HB8 / ATCC 27634 / DSM 579 / Gene: TTHA1784 Production host: ![]() ![]() References: UniProt: Q5SHE6 | ||
#4: Chemical | ChemComp-OLC / ( #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.26 Å3/Da / Density % sol: 62.25 % |
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Crystal grow | Temperature: 293 K / Method: lipidic cubic phase / pH: 6.5 / Details: PEG 500MME, MgSO4, Na2SO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX225HE / Detector: CCD / Date: Jan 20, 2015 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 21452 / % possible obs: 94.5 % / Redundancy: 4.7 % / Net I/σ(I): 10.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2ZJS Resolution: 2.724→43.943 Å / SU ML: 0.4 / Cross valid method: NONE / σ(F): 1.47 / Phase error: 26.03 / 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: 2.724→43.943 Å
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Refine LS restraints |
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LS refinement shell |
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