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- PDB-6ghz: Structure of Lytic Transglycosylase MltE mutant Y192F from E.coli -
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Open data
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Basic information
Entry | Database: PDB / ID: 6ghz | ||||||
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Title | Structure of Lytic Transglycosylase MltE mutant Y192F from E.coli | ||||||
![]() | Endo-type membrane-bound lytic murein transglycosylase A | ||||||
![]() | LYASE / Lytic Transglycosylase | ||||||
Function / homology | ![]() : / lytic endotransglycosylase activity / lytic transglycosylase activity / peptidoglycan metabolic process / cell outer membrane / cell wall organization / cell wall macromolecule catabolic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Batuecas, M.T. / Hermoso, J.A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: A Structural Dissection of the Active Site of the Lytic Transglycosylase MltE from Escherichia coli. Authors: Dik, D.A. / Batuecas, M.T. / Lee, M. / Mahasenan, K.V. / Marous, D.R. / Lastochkin, E. / Fisher, J.F. / Hermoso, J.A. / Mobashery, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 84.2 KB | Display | ![]() |
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PDB format | ![]() | 64.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.1 KB | Display | ![]() |
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Full document | ![]() | 442.3 KB | Display | |
Data in XML | ![]() | 15.8 KB | Display | |
Data in CIF | ![]() | 21.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ghyC ![]() 6gi3C ![]() 6gi4C ![]() 2y8pS 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: 21398.311 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: emtA, mltE, sltZ, ycgP, b1193, JW5821 / Production host: ![]() ![]() References: UniProt: P0C960, Lyases; Carbon-oxygen lyases; Acting on polysaccharides #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.06 % |
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Crystal grow | Temperature: 291 K / Method: microbatch / pH: 8.4 Details: 26% Polyethylene Glycol 4000, 0.2 M magnesium chloride and 0.1 M TRIS HCl (pH 8.4) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Jul 19, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97921 Å / Relative weight: 1 |
Reflection | Resolution: 2.33→45.38 Å / Num. obs: 17052 / % possible obs: 99.74 % / Redundancy: 9.7 % / Rpim(I) all: 0.024 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 2.33→2.41 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2Y8P Resolution: 2.33→45.38 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.916 / SU B: 0.007 / SU ML: 0 / Cross valid method: THROUGHOUT / ESU R: 0.236 / ESU R Free: 0.307 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||
Displacement parameters | Biso mean: 70.391 Å2
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Refinement step | Cycle: 1 / Resolution: 2.33→45.38 Å
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LS refinement shell | Resolution: 2.33→2.391 Å / Total num. of bins used: 20
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