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- PDB-4cn1: GlgE isoform 1 from Streptomyces coelicolor D394A mutant with mal... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4cn1 | |||||||||
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Title | GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound | |||||||||
![]() | ALPHA-1,4-GLUCAN\: MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE 1 | |||||||||
![]() | HYDROLASE / ALPHA-GLUCAN BIOSYNTHESIS / GLYCOSIDE HYDROLASE FAMILY 13_3 / DRUG TARGET | |||||||||
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. / Rashid, A.M. / Saalbach, G. / Tang, M. / Tuukanen, A. / Svergun, D.I. / Withers, S.G. / Lawson, D.M. / Bornemann, S. | |||||||||
![]() | ![]() 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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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BE" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BE" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 525.8 KB | Display | ![]() |
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PDB format | ![]() | 432.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 47.5 KB | Display | |
Data in CIF | ![]() | 69.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4cn4C ![]() 4cn6C ![]() 3zssS 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: 77520.836 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9L1K2, starch synthase (maltosyl-transferring) #2: Polysaccharide | #3: Water | ChemComp-HOH / | Sequence details | INCLUDES AN ADDITIONAL 20 RESIDUES AT THE N-TERMINUS FOR NICKEL AFFINITY PURIFICATION. RESIDUE 394 ...INCLUDES AN ADDITIONAL | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 11, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 2.55→104.53 Å / Num. obs: 67726 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 14 % / Biso Wilson estimate: 54.1 Å2 / Rmerge(I) obs: 0.17 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 2.55→2.62 Å / Redundancy: 13.7 % / Rmerge(I) obs: 0.66 / Mean I/σ(I) obs: 3 / % possible all: 96.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3ZSS Resolution: 2.55→91.95 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.923 / SU B: 14.495 / SU ML: 0.163 / Cross valid method: THROUGHOUT / ESU R: 0.343 / ESU R Free: 0.229 / 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: 45 Å2
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Refinement step | Cycle: LAST / Resolution: 2.55→91.95 Å
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Refine LS restraints |
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