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Yorodumi- PDB-8v4g: X-ray structure of the NADP-dependent reductase from Campylobacte... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8v4g | |||||||||
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Title | X-ray structure of the NADP-dependent reductase from Campylobacter jejuni responsible for the synthesis of CDP-glucitol in the presence of CDP and NADP | |||||||||
Components | Putative nucleotide sugar dehydratase | |||||||||
Keywords | OXIDOREDUCTASE / capsular polysaccharide / short chain dehydrogenase | |||||||||
Function / homology | NAD-dependent epimerase/dehydratase / NAD dependent epimerase/dehydratase family / NAD(P)-binding domain superfamily / CYTIDINE-5'-DIPHOSPHATE / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Putative nucleotide sugar dehydratase Function and homology information | |||||||||
Biological species | Campylobacter jejuni (Campylobacter) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | |||||||||
Authors | Schumann, M.E. / Thoden, J.B. / Holden, H.M. / Raushel, F.M. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Biochemistry / Year: 2024 Title: Biosynthesis of Cytidine Diphosphate-6-d-Glucitol for the Capsular Polysaccharides of Campylobacter jejuni. Authors: Ghosh, M.K. / Narindoshvili, T. / Thoden, J.B. / Schumann, M.E. / Holden, H.M. / Raushel, F.M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8v4g.cif.gz | 155.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8v4g.ent.gz | 119.8 KB | Display | PDB format |
PDBx/mmJSON format | 8v4g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8v4g_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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Full document | 8v4g_full_validation.pdf.gz | 1.7 MB | Display | |
Data in XML | 8v4g_validation.xml.gz | 28.3 KB | Display | |
Data in CIF | 8v4g_validation.cif.gz | 39.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v4/8v4g ftp://data.pdbj.org/pub/pdb/validation_reports/v4/8v4g | HTTPS FTP |
-Related structure data
Related structure data | 8v4hC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 38876.953 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Campylobacter jejuni (Campylobacter) / Strain: HS:5 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta2 / References: UniProt: A0A0U3AP28 |
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-Non-polymers , 5 types, 245 molecules
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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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: 2.35 Å3/Da / Density % sol: 47.66 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9 Details: protein incubated with 5 mM CDP and 5 mM NADP. Precipitant: 10-14 % w/v poly(ethylene glycol) 8000, 2% v/v hexyleneglycol, and 100 mM CHES (pH 9.0) |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SEALED TUBE / Type: BRUKER D8 QUEST / Wavelength: 1.54178 Å |
Detector | Type: Bruker PHOTON II / Detector: PIXEL / Date: Apr 5, 2023 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 49653 / % possible obs: 98.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 11.8 % / Rsym value: 0.094 / Net I/σ(I): 16.5 |
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 5.1 % / Mean I/σ(I) obs: 2.6 / Num. unique obs: 6294 / Rsym value: 0.46 / % possible all: 94.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→43.05 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.907 / SU B: 5.187 / SU ML: 0.139 / Cross valid method: THROUGHOUT / ESU R: 0.191 / ESU R Free: 0.181 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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 / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.348 Å2
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Refinement step | Cycle: 1 / Resolution: 2→43.05 Å
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Refine LS restraints |
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