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- PDB-6gfl: Crystal structure of the Escherichia coli nucleosidase PpnN (apo form) -
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Open data
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Basic information
Entry | Database: PDB / ID: 6gfl | ||||||
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Title | Crystal structure of the Escherichia coli nucleosidase PpnN (apo form) | ||||||
![]() | Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase | ||||||
![]() | HYDROLASE / YgdH / PpnN / allosteric enzyme / nucleotide metabolism / stringent response / antibiotic tolerance / persistence / fluoroquinolone | ||||||
Function / homology | ![]() inosinate nucleosidase activity / pyrimidine-5'-nucleotide nucleosidase / pyrimidine-5'-nucleotide nucleosidase activity / AMP nucleosidase / AMP nucleosidase activity / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds / guanosine tetraphosphate binding / protein-containing complex / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Zhang, Y. / Baerentsen, R.L. / Gerdes, K. / Brodersen, D.E. | ||||||
Funding support | ![]()
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![]() | ![]() Title: (p)ppGpp Regulates a Bacterial Nucleosidase by an Allosteric Two-Domain Switch. Authors: Zhang, Y.E. / Baerentsen, R.L. / Fuhrer, T. / Sauer, U. / Gerdes, K. / Brodersen, D.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 360.8 KB | Display | ![]() |
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PDB format | ![]() | 294 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.7 KB | Display | ![]() |
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Full document | ![]() | 458.7 KB | Display | |
Data in XML | ![]() | 33.7 KB | Display | |
Data in CIF | ![]() | 46.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6gfmC ![]() 2pmbS C: citing same article ( 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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Unit cell |
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Components
#1: Protein | Mass: 53244.168 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: ppnN, ygdH, b2795, JW2766 / Plasmid: pCA24N / Production host: ![]() ![]() References: UniProt: P0ADR8, Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds, pyrimidine-5'-nucleotide nucleosidase, AMP nucleosidase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 57.08 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1M HEPES pH 7.5 36% v/v PEG200 5 mg/ml protein concentration |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 30, 2017 Details: Oxford Danfysik/SESO Two stage demagnification using two K-B pairs of bimorph type mirrors |
Radiation | Monochromator: ACCEL Fixed exit Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9686 Å / Relative weight: 1 |
Reflection | Resolution: 2.48→49.08 Å / Num. obs: 38638 / % possible obs: 99.92 % / Redundancy: 13.4 % / Biso Wilson estimate: 65.26 Å2 / CC1/2: 0.99 / Rmerge(I) obs: 0.13 / Rpim(I) all: 0.03 / Rrim(I) all: 0.13 / Net I/σ(I): 12.97 |
Reflection shell | Resolution: 2.48→2.57 Å / Redundancy: 7.4 % / Rmerge(I) obs: 1.74 / Mean I/σ(I) obs: 1.15 / Num. unique obs: 3781 / CC1/2: 0.56 / Rpim(I) all: 0.68 / Rrim(I) all: 1.87 / % possible all: 99.95 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2PMB Resolution: 2.48→49.08 Å / Cross valid method: FREE R-VALUE
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Refinement step | Cycle: LAST / Resolution: 2.48→49.08 Å
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