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Yorodumi- PDB-6h8l: Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis -
+Open data
-Basic information
Entry | Database: PDB / ID: 6h8l | ||||||
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Title | Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis | ||||||
Components | Peptidoglycan-N-acetylmuramic acid deacetylase PdaC | ||||||
Keywords | HYDROLASE / Deacetylase | ||||||
Function / homology | Function and homology information hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / carbohydrate metabolic process / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Bacillus subtilis subsp. subtilis str. 168 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.54 Å | ||||||
Authors | Sainz-Polo, M.A. / Grifoll-Romero, L. / Albesa-Jove, D. / Planas, A. / Guerin, M.E. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2019 Title: Structure-function relationships underlying the dualN-acetylmuramic andN-acetylglucosamine specificities of the bacterial peptidoglycan deacetylase PdaC. Authors: Grifoll-Romero, L. / Sainz-Polo, M.A. / Albesa-Jove, D. / Guerin, M.E. / Biarnes, X. / Planas, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6h8l.cif.gz | 106.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6h8l.ent.gz | 79.6 KB | Display | PDB format |
PDBx/mmJSON format | 6h8l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h8/6h8l ftp://data.pdbj.org/pub/pdb/validation_reports/h8/6h8l | HTTPS FTP |
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-Related structure data
Related structure data | 6h8nC 2c1gS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 24514.756 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis subsp. subtilis str. 168 (bacteria) Gene: pdaC, yjeA, BSU12100 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: O34798, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.76 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.6 Details: 0.2 M ammonium tartrate dibasic pH 6.6, 20% (w/v) polyethylene glycol 3.350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9796 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 28, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9796 Å / Relative weight: 1 |
Reflection | Resolution: 1.54→56.07 Å / Num. obs: 67783 / % possible obs: 100 % / Redundancy: 6.5 % / Biso Wilson estimate: 17.77 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.0877 / Rrim(I) all: 0.0957 / Net I/σ(I): 11.39 |
Reflection shell | Resolution: 1.54→1.59 Å / Redundancy: 6.7 % / Rmerge(I) obs: 0.8135 / Mean I/σ(I) obs: 2.04 / Num. unique obs: 6689 / CC1/2: 0.713 / Rrim(I) all: 0.8819 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2C1G Resolution: 1.54→56.07 Å / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 17.9
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.24 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.54→56.07 Å
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Refine LS restraints |
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LS refinement shell |
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