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- PDB-5lgv: GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked i... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5lgv | ||||||||||||
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Title | GlgE isoform 1 from Streptomyces coelicolor E423A mutant soaked in maltooctaose | ||||||||||||
![]() | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 | ||||||||||||
![]() | TRANSFERASE / hydrolase / alpha-glucan biosynthesis / glycoside hydrolase family 13_3 | ||||||||||||
Function / homology | ![]() starch synthase (maltosyl-transferring) / alpha-glucan biosynthetic process / hexosyltransferase activity / oligosaccharide catabolic process / alpha-amylase activity Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Syson, K. / Stevenson, C.E.M. / Mia, F. / Barclay, J.E. / Tang, M. / Gorelik, A. / Rashid, A.M. / Lawson, D.M. / Bornemann, S. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Ligand-bound structures and site-directed mutagenesis identify the acceptor and secondary binding sites of Streptomyces coelicolor maltosyltransferase GlgE. Authors: Syson, K. / Stevenson, C.E. / Miah, F. / Barclay, J.E. / Tang, M. / Gorelik, A. / Rashid, A.M. / Lawson, D.M. / Bornemann, S. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 537.1 KB | Display | ![]() |
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PDB format | ![]() | 443.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 48.6 KB | Display | |
Data in CIF | ![]() | 70.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5cvsC ![]() 5lgwC ![]() 4cn6S S: Starting model for refinement C: citing same article ( |
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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: 77506.812 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: E423A variant expressed with a twenty residue nickel affinity tag with sequence MGSSHHHHHHSSGLVPRGSH appended to the N-terminus of the full-length amino acid sequence being derived from the pET-15b vector Source: (gene. exp.) ![]() Strain: ATCC BAA-471 / A3(2) / M145 / Gene: glgE1, pep1, pep1A, pep1I, SCO5443, SC6A11.19c / Plasmid: pET15b / Production host: ![]() ![]() References: UniProt: Q9L1K2, starch synthase (maltosyl-transferring) #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.27 Å3/Da / Density % sol: 62.33 % / Description: NULL |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: NULL |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Aug 1, 2014 | |||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 | |||||||||||||||||||||
Reflection | Resolution: 2.5→49.92 Å / Num. obs: 72101 / % possible obs: 100 % / Redundancy: 13 % / Biso Wilson estimate: 50.9 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.094 / Net I/av σ(I): 17.9 / Net I/σ(I): 17.9 | |||||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4CN6 Resolution: 2.5→49.92 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.95 / SU B: 16.796 / SU ML: 0.185 / SU R Cruickshank DPI: 0.3029 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.303 / ESU R Free: 0.212 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 149.66 Å2 / Biso mean: 65.669 Å2 / Biso min: 30.13 Å2
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Refinement step | Cycle: final / Resolution: 2.5→49.92 Å
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Refine LS restraints |
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