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- PDB-1ghk: SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEH... -
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Basic information
Entry | Database: PDB / ID: 1ghk | ||||||
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Title | SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, 25 STRUCTURES | ||||||
![]() | E2, THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX | ||||||
![]() | ACYLTRANSFERASE / GLYCOLYSIS / TRANSFERASE / LIPOYL | ||||||
Function / homology | ![]() L-lysine catabolic process to acetyl-CoA via saccharopine / dihydrolipoyllysine-residue succinyltransferase / dihydrolipoyllysine-residue succinyltransferase activity / oxoglutarate dehydrogenase complex / tricarboxylic acid cycle / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Berg, A. / Vervoort, J. / De Kok, A. | ||||||
![]() | ![]() Title: Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Authors: Berg, A. / Vervoort, J. / de Kok, A. #1: ![]() Title: Sequential 1H and 15N Nuclear Magnetic Resonance Assignments and Secondary Structure of the Lipoyl Domain of the 2-Oxoglutarate Dehydrogenase Complex from Azotobacter Vinelandii. Evidence for ...Title: Sequential 1H and 15N Nuclear Magnetic Resonance Assignments and Secondary Structure of the Lipoyl Domain of the 2-Oxoglutarate Dehydrogenase Complex from Azotobacter Vinelandii. Evidence for High Structural Similarity with the Lipoyl Domain of the Pyruvate Dehydrogenase Complex Authors: Berg, A. / Smits, O. / De Kok, A. / Vervoort, J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 565.8 KB | Display | ![]() |
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PDB format | ![]() | 474.5 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 343.8 KB | Display | ![]() |
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Full document | ![]() | 525 KB | Display | |
Data in XML | ![]() | 40.9 KB | Display | |
Data in CIF | ![]() | 63 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 8353.437 Da / Num. of mol.: 1 / Fragment: LIPOYL DOMAIN, RESIDUES 1-79 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P20708, dihydrolipoyllysine-residue succinyltransferase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 25 |