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- PDB-1qjo: INNERMOST LIPOYL DOMAIN OF THE PYRUVATE DEHYDROGENASE FROM ESCHER... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qjo | ||||||
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Title | INNERMOST LIPOYL DOMAIN OF THE PYRUVATE DEHYDROGENASE FROM ESCHERICHIA COLI | ||||||
![]() | DIHYDROLIPOAMIDE ACETYLTRANSFERASE | ||||||
![]() | DIHYDROLIPOAMIDE ACETYLTRANSFERASE / LIPOYL DOMAIN / PYRUVATE DEHYDROGENASE | ||||||
Function / homology | ![]() pyruvate catabolic process / dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / acetyl-CoA biosynthetic process from pyruvate / lipoic acid binding / pyruvate dehydrogenase complex / pyruvate metabolic process / acetyltransferase activity / glycolytic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / XPLOR | ||||||
![]() | Jones, D.D. / Howard, M.J. / Perham, R.N. | ||||||
![]() | ![]() Title: Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli. Authors: Jones, D.D. / Stott, K.M. / Howard, M.J. / Perham, R.N. #1: Journal: J.Mol.Biol. / Year: 2000 Title: Protein-Protein Interaction Revealed by NMR T(2) Relaxation Experiments: The Lipoyl Domain and E1 Component of the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus Stearothermophilus Authors: Howard, M.J. / Chauhan, H.J. / Domingo, G.J. / Fuller, C. / Perham, R.N. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 682.5 KB | Display | ![]() |
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PDB format | ![]() | 572.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 353.6 KB | Display | ![]() |
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Full document | ![]() | 561.5 KB | Display | |
Data in XML | ![]() | 44.3 KB | Display | |
Data in CIF | ![]() | 71.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 8380.669 Da / Num. of mol.: 1 / Fragment: LIPOAMIDE BINDING DOMAIN OF E2P Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 90% H2O/ 10%D2O |
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Sample conditions | Ionic strength: 20MM NAPI / pH: 5.5 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AM / Manufacturer: Bruker / Model: AM / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: XPLOR / Software ordinal: 1 Details: THE N-TERMINAL MET IS AN ARTIFACT OF THE EXPRESSION SYSTEM USED AND NO RESTRAINTS WERE USED TO CALCULATE ITS PART IN THE STRUCTURE. | ||||||||||||
NMR ensemble | Conformers calculated total number: 60 / Conformers submitted total number: 30 |