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- PDB-1lab: THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS ST... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lab | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX | ||||||
![]() | DIHYDROLIPOAMIDE ACETYLTRANSFERASE | ||||||
![]() | TRANSFERASE (ACYLTRANSFERASE) | ||||||
Function / homology | ![]() dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / lipoic acid binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Dardel, F. / Davis, A.L. / Laue, E.D. / Perham, R.N. | ||||||
![]() | ![]() Title: Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex. Authors: Dardel, F. / Davis, A.L. / Laue, E.D. / Perham, R.N. #1: ![]() Title: Sequence-Specific 1H-NMR Assignments and Secondary Structure of the Lipoyl Domain of the Bacillus Stearothermophilus Pyruvate Dehydrogenase Multienzyme Complex Authors: Dardel, F. / Laue, E.D. / Perham, R.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 267 KB | Display | ![]() |
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PDB format | ![]() | 219.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 352.8 KB | Display | ![]() |
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Full document | ![]() | 438.6 KB | Display | |
Data in XML | ![]() | 20.1 KB | Display | |
Data in CIF | ![]() | 31 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: 8653.785 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: BACILLUS STEAROTHERMOPHILUS / Gene (production host): BACILLUS STEAROTHERMOPHILUS References: UniProt: P11961, dihydrolipoyllysine-residue acetyltransferase |
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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
Software |
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NMR software | Name: ![]() | ||||||||
NMR ensemble | Conformers submitted total number: 11 |