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Yorodumi- PDB-1ghj: SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEH... -
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Basic information
| Entry | Database: PDB / ID: 1ghj | ||||||
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| Title | SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
Components | E2, THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX | ||||||
Keywords | ACYLTRANSFERASE / GLYCOLYSIS / TRANSFERASE / LIPOYL | ||||||
| Function / homology | Function and homology informationL-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 | Azotobacter vinelandii (bacteria) | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Berg, A. / Vervoort, J. / De Kok, A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996Title: Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Authors: Berg, A. / Vervoort, J. / de Kok, A. #1: Journal: Eur.J.Biochem. / Year: 1995Title: 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: Molmil Jmol/JSmol |
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Download
| PDBx/mmCIF format | 1ghj.cif.gz | 35.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1ghj.ent.gz | 24.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1ghj.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1ghj_validation.pdf.gz | 333.4 KB | Display | wwPDB validaton report |
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| Full document | 1ghj_full_validation.pdf.gz | 336.1 KB | Display | |
| Data in XML | 1ghj_validation.xml.gz | 3.4 KB | Display | |
| Data in CIF | 1ghj_validation.cif.gz | 4.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gh/1ghj ftp://data.pdbj.org/pub/pdb/validation_reports/gh/1ghj | HTTPS FTP |
-Related structure data
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Assembly
| Deposited unit | ![]()
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| 1 |
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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.) Azotobacter vinelandii (bacteria) / Production host: ![]() 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: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement | ||||||||||||
| NMR ensemble | Conformers submitted total number: 1 |
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