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Yorodumi- PDB-4cn4: GlgE isoform 1 from Streptomyces coelicolor E423A mutant with 2-d... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4cn4 | |||||||||
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Title | GlgE isoform 1 from Streptomyces coelicolor E423A mutant with 2-deoxy- 2-fluoro-beta-maltosyl modification | |||||||||
Components | ALPHA-1,4-GLUCAN\:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE 1 | |||||||||
Keywords | TRANSFERASE / ALPHA-GLUCAN BIOSYNTHESIS / GLYCOSIDE HYDROLASE FAMILY 13_3 / DRUG TARGET | |||||||||
Function / homology | Function and homology information starch synthase (maltosyl-transferring) / alpha-glucan biosynthetic process / oligosaccharide catabolic process / hexosyltransferase activity / alpha-amylase activity Similarity search - Function | |||||||||
Biological species | STREPTOMYCES COELICOLOR (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | |||||||||
Authors | Syson, K. / Stevenson, C.E.M. / Rashid, A.M. / Saalbach, G. / Tang, M. / Tuukanen, A. / Svergun, D.I. / Withers, S.G. / Lawson, D.M. / Bornemann, S. | |||||||||
Citation | Journal: Biochemistry / Year: 2014 Title: Structural Insight Into How Streptomyces Coelicolor Maltosyl Transferase Glge Binds Alpha-Maltose 1-Phosphate and Forms a Maltosyl-Enzyme Intermediate. Authors: Syson, K. / Stevenson, C.E.M. / Rashid, A.M. / Saalbach, G. / Tang, M. / Tuukkanen, A. / Svergun, D.I. / Withers, S.G. / Lawson, D.M. / Bornemann, S. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4cn4.cif.gz | 525.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4cn4.ent.gz | 432.9 KB | Display | PDB format |
PDBx/mmJSON format | 4cn4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cn/4cn4 ftp://data.pdbj.org/pub/pdb/validation_reports/cn/4cn4 | HTTPS FTP |
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-Related structure data
Related structure data | 4cn1C 4cn6C 3zssS 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: 77506.812 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) STREPTOMYCES COELICOLOR (bacteria) / Strain: M145 / Plasmid: PET15B-GLGE1-M145 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS References: UniProt: Q9L1K2, starch synthase (maltosyl-transferring) #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Water | ChemComp-HOH / | Sequence details | INCLUDES AN ADDITIONAL 20 RESIDUES AT THE N-TERMINUS FOR NICKEL AFFINITY PURIFICATION. RESIDUE 423 ...INCLUDES AN ADDITIONAL | |
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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: 3.26 Å3/Da / Density % sol: 62.3 % / Description: NONE |
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Crystal grow | pH: 7 / Details: pH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.917 |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jan 30, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.917 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50.54 Å / Num. obs: 79517 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 7.3 % / Biso Wilson estimate: 43.7 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 14.7 |
Reflection shell | Resolution: 2.4→2.47 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.99 / Mean I/σ(I) obs: 2 / % possible all: 95.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3ZSS Resolution: 2.4→50.54 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.947 / SU B: 12.12 / SU ML: 0.143 / Cross valid method: THROUGHOUT / ESU R: 0.257 / ESU R Free: 0.192 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
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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: 53 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→50.54 Å
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Refine LS restraints |
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