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- PDB-5jxx: Crystal structure of UDP-N-acetylglucosamine O-acyltransferase (L... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5jxx | ||||||
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Title | Crystal structure of UDP-N-acetylglucosamine O-acyltransferase (LpxA) from Moraxella catarrhalis RH4. | ||||||
![]() | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | ||||||
![]() | TRANSFERASE / UDP-N-acetylglucosamine O-acyltransferase / LpxA / acyltransferase | ||||||
Function / homology | ![]() acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase / acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity / lipid A biosynthetic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Pratap, S. / Kesari, P. / Yadav, R. / Narwal, M. / Dev, A. / Kumar, P. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Acyl chain preference and inhibitor identification of Moraxella catarrhalis LpxA: Insight through crystal structure and computational studies. Authors: Pratap, S. / Kesari, P. / Yadav, R. / Dev, A. / Narwal, M. / Kumar, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 296.5 KB | Display | ![]() |
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PDB format | ![]() | 242 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 501.6 KB | Display | ![]() |
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Full document | ![]() | 523.7 KB | Display | |
Data in XML | ![]() | 54.9 KB | Display | |
Data in CIF | ![]() | 71.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4e6uS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 28040.043 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: BBH18 / Gene: lpxA, MCR_0549 Production host: ![]() ![]() References: UniProt: D5VAW8, acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase #2: Chemical | ChemComp-GOL / #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 58.06 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5 Details: 0.05 M Citric Bis-Tris, Propane, pH 5.0, 16% (w/v) Polyethylene glycol 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: May 20, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 3→45.39 Å / Num. obs: 30503 / % possible obs: 80 % / Redundancy: 2.7 % / Net I/σ(I): 4.76 |
Reflection shell | Resolution: 3.001→3.108 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4E6U Resolution: 3.001→45.39 Å / SU ML: 0.44 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 31.29 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.001→45.39 Å
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Refine LS restraints |
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LS refinement shell |
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