[English] 日本語
Yorodumi- PDB-1w4h: Peripheral-subunit from mesophilic, thermophilic and hyperthermop... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1w4h | ||||||
---|---|---|---|---|---|---|---|
Title | Peripheral-subunit from mesophilic, thermophilic and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions | ||||||
Components | DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASEDihydrolipoyl transacetylase | ||||||
Keywords | TRANSFERASE / ULTRAFAST FOLDING / HOMOLOGUES / PERIPHERAL-SUBUNIT BINDING DOMAINS | ||||||
Function / homology | Function and homology information L-lysine catabolic process to acetyl-CoA via saccharopine / oxoglutarate dehydrogenase complex / dihydrolipoyllysine-residue succinyltransferase / dihydrolipoyllysine-residue succinyltransferase activity / dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / lipoic acid binding / tricarboxylic acid cycle / glycolytic process / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Ferguson, N. / Sharpe, T.D. / Schartau, P.J. / Allen, M.D. / Johnson, C.M. / Fersht, A.R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1w4h.cif.gz | 265.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1w4h.ent.gz | 222 KB | Display | PDB format |
PDBx/mmJSON format | 1w4h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w4/1w4h ftp://data.pdbj.org/pub/pdb/validation_reports/w4/1w4h | HTTPS FTP |
---|
-Related structure data
Related structure data | 1w4eC 1w4fC 1w4gC 1w4iC 1w4jC 1w4kC 2btgC 2bthC C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-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.) ESCHERICHIA COLI (E. coli) / Plasmid: PRSETA / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) References: UniProt: P11961, UniProt: P0AFG6*PLUS, dihydrolipoyllysine-residue acetyltransferase |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|---|
NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C,15N LABELLED MATERIAL |
-Sample preparation
Details | Contents: 95%WATER/5% D20, 3MM SAMPLE |
---|---|
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 |
---|
-Processing
NMR software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |