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- PDB-1w4h: Peripheral-subunit from mesophilic, thermophilic and hyperthermop... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1w4h | ||||||
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Title | Peripheral-subunit from mesophilic, thermophilic and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions | ||||||
![]() | DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE | ||||||
![]() | TRANSFERASE / ULTRAFAST FOLDING / HOMOLOGUES / PERIPHERAL-SUBUNIT BINDING DOMAINS | ||||||
Function / homology | ![]() L-lysine catabolic process to acetyl-CoA via saccharopine / dihydrolipoyllysine-residue succinyltransferase / dihydrolipoyllysine-residue succinyltransferase activity / dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / oxoglutarate dehydrogenase complex / lipoic acid binding / tricarboxylic acid cycle / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Ferguson, N. / Sharpe, T.D. / Schartau, P.J. / Allen, M.D. / Johnson, C.M. / Fersht, A.R. | ||||||
![]() | ![]() Title: Ultra-Fast Barrier-Limited Folding in the Peripheral Subunit-Binding Domain Family. Authors: Ferguson, N. / Sharpe, T.D. / Schartau, P.J. / Sato, S. / Allen, M.D. / Johnson, C.M. / Rutherford, T.J. / Fersht, A.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 268.6 KB | Display | ![]() |
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PDB format | ![]() | 223.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 339.7 KB | Display | ![]() |
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Full document | ![]() | 449.8 KB | Display | |
Data in XML | ![]() | 16.8 KB | Display | |
Data in CIF | ![]() | 26.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1w4eC ![]() 1w4fC ![]() 1w4gC ![]() 1w4iC ![]() 1w4jC ![]() 1w4kC ![]() 2btgC ![]() 2bthC 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/peptide | Mass: 4960.547 Da / Num. of mol.: 1 / Fragment: RESIDUES 108-152 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P11961, UniProt: P0AFG6*PLUS, dihydrolipoyllysine-residue acetyltransferase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C,15N LABELLED MATERIAL |
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Sample preparation
Details | Contents: 95%WATER/5% D20, 3MM SAMPLE |
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Sample conditions | Ionic strength: 200 / pH: 7.0 / Pressure: 1.0 atm / Temperature: 298.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | |||||||||||||||
NMR ensemble | Conformer selection criteria: NO VIOLATIONS > 0.25 / Conformers calculated total number: 20 / Conformers submitted total number: 20 |