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Yorodumi- PDB-2btg: peripheral-subunit binding domains from mesophilic,thermophilic, ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2btg | ||||||
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Title | peripheral-subunit binding domains from mesophilic,thermophilic, and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions | ||||||
Components | DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX | ||||||
Keywords | TRANSFERASE / ACYLTRANSFERASE / LIPOYL | ||||||
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 / lipoic acid binding / tricarboxylic acid cycle / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Ferguson, N. / Allen, M.D. | ||||||
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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2btg.cif.gz | 269.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2btg.ent.gz | 232.8 KB | Display | PDB format |
PDBx/mmJSON format | 2btg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bt/2btg ftp://data.pdbj.org/pub/pdb/validation_reports/bt/2btg | HTTPS FTP |
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-Related structure data
Related structure data | 1w4eC 1w4fC 1w4gC 1w4hC 1w4iC 1w4jC 1w4kC 2bthC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 5008.610 Da / Num. of mol.: 1 / Fragment: RESIDUES 108-152 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 References: UniProt: P07016, UniProt: P0AFG6*PLUS, dihydrolipoyllysine-residue succinyltransferase | ||
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Compound details | ENGINEEREDSequence details | GLY-SER AT THE N-TERMINUS IS THE REMAINS OF A THROMBIN CLEAVAGE SITE. HIS TO TRP MUTATION IS A ...GLY-SER AT THE N-TERMINUS IS THE REMAINS OF A THROMBIN CLEAVAGE SITE. HIS TO TRP MUTATION IS A DELIBERATE | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR details | Text: NONE |
-Sample preparation
Details | Contents: 50 MM POTASSIUM PHOSPHATE, 10% D2O |
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Sample conditions | pH: 6.5 / Temperature: 298.0 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 / Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL ABOVE | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: ACCEPTED / Conformers calculated total number: 20 / Conformers submitted total number: 20 |