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Yorodumi- PDB-1ns7: Crystal structure of galactose mutarotase from Lactococcus lactis... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ns7 | ||||||
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Title | Crystal structure of galactose mutarotase from Lactococcus lactis mutant E304A complexed with glucose | ||||||
Components | GALACTOSE MUTAROTASE | ||||||
Keywords | ISOMERASE / MUTAROTASE / EPIMERASE / GALACTOSE METABOLISM | ||||||
Function / homology | Function and homology information aldose 1-epimerase / aldose 1-epimerase activity / galactose metabolic process / carbohydrate binding Similarity search - Function | ||||||
Biological species | Lactococcus lactis (lactic acid bacteria) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 1.85 Å | ||||||
Authors | Holden, H.M. / Thoden, J.B. | ||||||
Citation | Journal: Protein Sci. / Year: 2003 Title: The Catalytic Mechanism of Galactose Mutarotase Authors: Thoden, J.B. / Kim, J. / Raushel, F.M. / Holden, H.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ns7.cif.gz | 155.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ns7.ent.gz | 120.4 KB | Display | PDB format |
PDBx/mmJSON format | 1ns7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ns/1ns7 ftp://data.pdbj.org/pub/pdb/validation_reports/ns/1ns7 | HTTPS FTP |
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-Related structure data
Related structure data | 1ns0C 1ns2C 1ns4C 1ns8C 1nsmC 1nsrC 1nssC 1nsuC 1nsvC 1nsxC 1nszC 1l7jS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 38564.922 Da / Num. of mol.: 2 / Mutation: E304A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lactococcus lactis (lactic acid bacteria) Plasmid: PET28 / Production host: Escherichia coli (E. coli) / Strain (production host): ROSETTA / References: UniProt: Q9ZB17, aldose 1-epimerase #2: Sugar | #3: Chemical | ChemComp-NA / | #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: 2.22 Å3/Da / Density % sol: 44.06 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6 Details: MES, methylether-PEG-5000, NaCl, pH 6.00, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6 / Method: vapor diffusion | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54178 Å |
Detector | Type: SIEMENS HI-STAR / Detector: AREA DETECTOR / Date: Mar 3, 2002 / Details: GOEBEL MIRRORS |
Radiation | Monochromator: GOEBEL OPTICS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→30 Å / Num. all: 60611 / Num. obs: 60611 / % possible obs: 96.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Rsym value: 0.054 / Net I/σ(I): 13.6 |
Reflection shell | Resolution: 1.95→2.03 Å / Redundancy: 1.8 % / Mean I/σ(I) obs: 3.4 / Rsym value: 0.225 / % possible all: 74.2 |
Reflection | *PLUS Lowest resolution: 30 Å / Rmerge(I) obs: 0.0535 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: PDB ENTRY 1L7J Resolution: 1.85→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 1.85→30 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 30 Å / Num. reflection obs: 54496 / Rfactor obs: 0.17 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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