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- PDB-5n6l: Structure of the membrane integral lipoprotein N-acyltransferase ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5n6l | ||||||
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Title | Structure of the membrane integral lipoprotein N-acyltransferase Lnt C387A mutant from E. coli | ||||||
![]() | Apolipoprotein N-acyltransferase | ||||||
![]() | TRANSFERASE / membrane protein / lipoprotein / N-acyltransferase / lipidic cubic phase | ||||||
Function / homology | ![]() apolipoprotein N-acyltransferase / N-acyltransferase activity / lipoprotein biosynthetic process / outer membrane-bounded periplasmic space / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Huang, C.-Y. / Boland, C. / Howe, N. / Wiktor, M. / Vogeley, L. / Weichert, D. / Bailey, J. / Olieric, V. / Wang, M. / Caffrey, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis. Authors: Wiktor, M. / Weichert, D. / Howe, N. / Huang, C.Y. / Olieric, V. / Boland, C. / Bailey, J. / Vogeley, L. / Stansfeld, P.J. / Buddelmeijer, N. / Wang, M. / Caffrey, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 221.6 KB | Display | ![]() |
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PDB format | ![]() | 176.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5n6hSC ![]() 5n6mC 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 59248.695 Da / Num. of mol.: 2 / Mutation: C387A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: lnt, cutE, b0657, JW0654 / Cell (production host): C43 / Production host: ![]() ![]() References: UniProt: P23930, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups #2: Chemical | ChemComp-OLC / ( #3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.29 Å3/Da / Density % sol: 62.64 % |
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Crystal grow | Temperature: 293 K / Method: lipidic cubic phase Details: 8 % (v/v) MPD 0.1 M MES pH 6 0.4 M ammonium citrate 0.1 M sodium malonate pH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 14, 2016 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99998 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→49.79 Å / Num. obs: 34916 / % possible obs: 97.9 % / Redundancy: 5.4 % / Net I/σ(I): 7.72 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5N6H Resolution: 2.9→49.79 Å / SU ML: 0.44 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 28.36
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→49.79 Å
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Refine LS restraints |
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LS refinement shell |
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