+Open data
-Basic information
Entry | Database: PDB / ID: 7vss | ||||||
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Title | Phosphoglucomutase_tlr1976 | ||||||
Components | Phosphoglucomutase | ||||||
Keywords | UNKNOWN FUNCTION / phosphoglucomutase_tlr1976 | ||||||
Function / homology | Function and homology information phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) / phosphoglucomutase activity / carbohydrate metabolic process / magnesium ion binding Similarity search - Function | ||||||
Biological species | Thermosynechococcus elongatus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.96 Å | ||||||
Authors | Su, J.Y. | ||||||
Funding support | 1items
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Citation | Journal: To Be Published Title: phosphoglucomutase_tlr1976 Authors: Su, J.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7vss.cif.gz | 110.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7vss.ent.gz | 83.5 KB | Display | PDB format |
PDBx/mmJSON format | 7vss.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7vss_validation.pdf.gz | 432.1 KB | Display | wwPDB validaton report |
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Full document | 7vss_full_validation.pdf.gz | 437.3 KB | Display | |
Data in XML | 7vss_validation.xml.gz | 18.9 KB | Display | |
Data in CIF | 7vss_validation.cif.gz | 25.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vs/7vss ftp://data.pdbj.org/pub/pdb/validation_reports/vs/7vss | HTTPS FTP |
-Related structure data
Related structure data | 1kfqS S: Starting model for refinement |
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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
#1: Protein | Mass: 58830.145 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermosynechococcus elongatus (strain BP-1) (bacteria) Strain: BP-1 / Gene: tlr1976 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8DHI3 |
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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: 4.58 Å3/Da / Density % sol: 73.12 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: NaCl |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97915 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 2, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97915 Å / Relative weight: 1 |
Reflection | Resolution: 2.96→19.74 Å / Num. obs: 23412 / % possible obs: 99.7 % / Redundancy: 12.6 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 29 |
Reflection shell | Resolution: 2.96→3.14 Å / Rmerge(I) obs: 0.519 / Num. unique obs: 3703 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1kfq Resolution: 2.96→19.73 Å / SU ML: 0.35 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 23.96 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 145.43 Å2 / Biso mean: 75.0486 Å2 / Biso min: 30 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.96→19.73 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14 / % reflection obs: 100 %
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