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Open data
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Basic information
Entry | Database: PDB / ID: 6p24 | ||||||
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Title | Escherichia coli tRNA synthetase | ||||||
![]() | (Phenylalanine--tRNA ligase ...) x 2 | ||||||
![]() | LIGASE / Inhibitor / Aminoacyl-tRNA synthetase / PheRS / Antibacterial | ||||||
Function / homology | ![]() phenylalanine-tRNA ligase complex / phenylalanine-tRNA ligase / phenylalanine-tRNA ligase activity / phenylalanyl-tRNA aminoacylation / tRNA binding / magnesium ion binding / ATP binding / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kahne, D. / Baidin, V. / Owens, T.W. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Simple Secondary Amines Inhibit Growth of Gram-Negative Bacteria through Highly Selective Binding to Phenylalanyl-tRNA Synthetase. Authors: Baidin, V. / Owens, T.W. / Lazarus, M.B. / Kahne, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 549.2 KB | Display | ![]() |
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PDB format | ![]() | 354.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 312.2 KB | Display | ![]() |
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Full document | ![]() | 314 KB | Display | |
Data in XML | ![]() | 2.7 KB | Display | |
Data in CIF | ![]() | 26.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6oz5C ![]() 6p26C ![]() 6p8tC ![]() 3pcoS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Phenylalanine--tRNA ligase ... , 2 types, 4 molecules ACBD
#1: Protein | Mass: 37318.156 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: pheS, b1714, JW5277 / Production host: ![]() ![]() #2: Protein | Mass: 87483.039 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: pheT, b1713, JW1703 / Production host: ![]() ![]() |
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-Non-polymers , 8 types, 579 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HEZ.gif)
![](data/chem/img/TRS.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HEZ.gif)
![](data/chem/img/TRS.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-CL / | #5: Chemical | ChemComp-HEZ / #6: Chemical | ChemComp-TRS / #7: Chemical | ChemComp-PEG / #8: Chemical | ChemComp-EDO / #9: Chemical | #10: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.08 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 16% PEG 8,000, 200 mM MgCl2, 100 mM Tris-HCl pH8.5, 2% 1,6-hexanediol, 3% d-Galactose |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 14, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.115→173.58 Å / Num. obs: 152649 / % possible obs: 98.7 % / Redundancy: 3.3 % / Biso Wilson estimate: 50.86 Å2 / CC1/2: 0.994 / Net I/σ(I): 6.7 |
Reflection shell | Resolution: 2.115→2.15 Å / Num. unique obs: 6642 / CC1/2: 0.126 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3PCO Resolution: 2.12→82.04 Å / SU ML: 0.351 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 28.6791 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 60.39 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.12→82.04 Å
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Refine LS restraints |
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LS refinement shell |
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