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- PDB-4f9u: Structure of glycosylated glutaminyl cyclase from Drosophila mela... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4f9u | |||||||||
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Title | Structure of glycosylated glutaminyl cyclase from Drosophila melanogaster | |||||||||
![]() | CG32412 | |||||||||
![]() | ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Function / homology | ![]() peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase / ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Kolenko, P. / Koch, B. / Ruiz-Carilo, D. / Stubbs, M.T. | |||||||||
![]() | ![]() Title: Crystal Structures of Glutaminyl Cyclases (QCs) from Drosophila melanogaster Reveal Active Site Conservation between Insect and Mammalian QCs. Authors: Koch, B. / Kolenko, P. / Buchholz, M. / Ruiz Carrillo, D. / Parthier, C. / Wermann, M. / Rahfeld, J.U. / Reuter, G. / Schilling, S. / Stubbs, M.T. / Demuth, H.U. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 152.6 KB | Display | ![]() |
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PDB format | ![]() | 116.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4f9vC ![]() 4faiC ![]() 4fbeC ![]() 3si2S 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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2 | ![]()
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Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 35341.672 Da / Num. of mol.: 2 / Fragment: UNP residues 29-340 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() References: UniProt: Q9VRQ9, ![]() ![]() |
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-Sugars , 2 types, 2 molecules
#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose![]() Source method: isolated from a genetically manipulated source |
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#3: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose![]() Source method: isolated from a genetically manipulated source |
-Non-polymers , 4 types, 578 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/PBD.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PBD.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | #5: Chemical | #6: Chemical | ChemComp-GOL / | ![]() #7: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.65 % |
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Crystal grow![]() | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 10% PEG35000, 2 mM PQ50, 0.1 M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Jul 10, 2010 / Details: mirrors |
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.8→90.902 Å / Num. all: 57060 / Num. obs: 57047 / % possible obs: 99 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3.7 / Redundancy: 4.2 % / Biso Wilson estimate: 18 Å2 / Rmerge(I) obs: 0.079 / Net I/σ(I): 10.6 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.514 / Mean I/σ(I) obs: 2.2 / Num. unique all: 8206 / % possible all: 97.8 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 3SI2 Resolution: 1.8→90.9 Å / Cor.coef. Fo:Fc: 0.96 / SU B: 2.277 / SU ML: 0.071 / Isotropic thermal model: ISOTROPIC / Cross valid method: THROUGHOUT / ESU R: 0.124 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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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: 17.772 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→90.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.847 Å / Total num. of bins used: 20
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