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- PDB-5jto: The structure of chaperone SecB in complex with unstructured proP... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5jto | ||||||
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Title | The structure of chaperone SecB in complex with unstructured proPhoA binding site d | ||||||
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![]() | CHAPERONE/HYDROLASE / Molecular chaperone / CHAPERONE-HYDROLASE complex | ||||||
Function / homology | ![]() preprotein binding / maintenance of unfolded protein / oxidoreductase activity, acting on phosphorus or arsenic in donors / protein transport by the Sec complex / alkaline phosphatase / alkaline phosphatase activity / hydrogenase (acceptor) activity / phosphoprotein phosphatase activity / localization / protein targeting ...preprotein binding / maintenance of unfolded protein / oxidoreductase activity, acting on phosphorus or arsenic in donors / protein transport by the Sec complex / alkaline phosphatase / alkaline phosphatase activity / hydrogenase (acceptor) activity / phosphoprotein phosphatase activity / localization / protein targeting / dephosphorylation / protein dephosphorylation / protein tetramerization / protein localization / unfolded protein binding / protein transport / protein folding / outer membrane-bounded periplasmic space / periplasmic space / magnesium ion binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
![]() | Huang, C. / Saio, T. / Rossi, P. / Kalodimos, C.G. | ||||||
![]() | ![]() Title: Structural basis for the antifolding activity of a molecular chaperone. Authors: Huang, C. / Rossi, P. / Saio, T. / Kalodimos, C.G. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 5.2 MB | Display | ![]() |
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PDB format | ![]() | 4.4 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 651.7 KB | Display | ![]() |
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Full document | ![]() | 2.6 MB | Display | |
Data in XML | ![]() | 608.5 KB | Display | |
Data in CIF | ![]() | 578 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5jtlC ![]() 5jtmC ![]() 5jtnC ![]() 5jtpC ![]() 5jtqC ![]() 5jtrC 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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NMR ensembles |
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Components
#1: Protein | Mass: 17287.266 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 4325.987 Da / Num. of mol.: 4 / Fragment: residues 271-310 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: phoA, b0383, JW0374 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 300 uM [U-100% 13C; U-100% 15N] E.coli chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Alkaline Phosphatase (PhoA) binding site d, 150 mM potassium chloride, 50 mM sodium phosphate, ...Contents: 300 uM [U-100% 13C; U-100% 15N] E.coli chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Alkaline Phosphatase (PhoA) binding site d, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O Details: 1H,13C-ILVMAT methyl labelling otherwise uniformly deuterated, 12C and 15N Specific labelling of aromatic residues Label: Sample_1 / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 150 mM / Label: condition_1 / pH: 7 / Pressure: 1 atm / Temperature: 301 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |