[English] 日本語
Yorodumi- PDB-1qjo: INNERMOST LIPOYL DOMAIN OF THE PYRUVATE DEHYDROGENASE FROM ESCHER... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qjo | ||||||
---|---|---|---|---|---|---|---|
Title | INNERMOST LIPOYL DOMAIN OF THE PYRUVATE DEHYDROGENASE FROM ESCHERICHIA COLI | ||||||
Components | DIHYDROLIPOAMIDE ACETYLTRANSFERASEDihydrolipoyl transacetylase | ||||||
Keywords | DIHYDROLIPOAMIDE ACETYLTRANSFERASE / LIPOYL DOMAIN / PYRUVATE DEHYDROGENASE | ||||||
Function / homology | Function and homology information 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 | ESCHERICHIA COLI BL21 (bacteria) | ||||||
Method | SOLUTION NMR / XPLOR | ||||||
Authors | Jones, D.D. / Howard, M.J. / Perham, R.N. | ||||||
Citation | Journal: Biochemistry / Year: 2000 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. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1qjo.cif.gz | 679.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1qjo.ent.gz | 593.3 KB | Display | PDB format |
PDBx/mmJSON format | 1qjo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qj/1qjo ftp://data.pdbj.org/pub/pdb/validation_reports/qj/1qjo | HTTPS FTP |
---|
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-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.) ESCHERICHIA COLI BL21(DE3) (bacteria) / Cellular location: CYTOPLASM / Gene: E2P_ECOLI / Plasmid: PET11C / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P06959 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 90% H2O/ 10%D2O |
---|---|
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 |
---|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |