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Open data
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Basic information
Entry | Database: PDB / ID: 8pek | |||||||||
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Title | Structure of the dimeric, periplasmic domain of ExbD | |||||||||
![]() | Biopolymer transport protein ExbD | |||||||||
![]() | TRANSPORT PROTEIN / ton / tonb-binding / exbb-integrated / periplasmic / exbb-exbd / dimer | |||||||||
Function / homology | TonB system transport protein ExbD type-1 / Biopolymer transport protein ExbD/TolR / Biopolymer transport protein ExbD/TolR / transmembrane transporter activity / protein transport / membrane => GO:0016020 / plasma membrane / Biopolymer transport protein ExbD![]() | |||||||||
Biological species | ![]() | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
![]() | Zinke, M. / Bardiaux, B. / Izadi-Pruneyre, N. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Ton motor conformational switch and peptidoglycan role in bacterial nutrient uptake. Authors: Zinke, M. / Lejeune, M. / Mechaly, A. / Bardiaux, B. / Boneca, I.G. / Delepelaire, P. / Izadi-Pruneyre, N. #1: Journal: Biorxiv / Year: 2023 Title: Ton Motor Conformational Switch and Peptidoglycan Role in Bacterial Nutrient Uptake. Authors: Zinke, M. / Lejeune, M. / Mechaly, A. / Bardiaux, B. / Boneca, I.G. / Delepelaire, P. / Izadi-Pruneyre, 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 | ![]() | 650.2 KB | Display | ![]() |
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PDB format | ![]() | 550.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 547.1 KB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 158.4 KB | Display | |
Data in CIF | ![]() | 161.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8p9rC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
Other databases |
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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: 10870.383 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: exbD, AN695_0216350, AR325_24260, BVG93_18405, BVG97_18665, C3R40_07870, CHR63_10945, DMW43_16865, FOT62_00910, HMI62_22190, HP475_23720 Plasmid: pet30(a)+ / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 0.3 mM / Label: conditions_1 / pH: 7 / Pressure: 1 atm / Temperature: 293.15 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 2 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: medoid | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 10 |