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Open data
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Basic information
Entry | Database: PDB / ID: 1c90 | ||||||
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Title | Endo-Beta-N-Acetylglucosaminidase H, E132Q Mutant | ||||||
![]() | ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H | ||||||
![]() | HYDROLASE / (BETA/ALPHA)8 BARREL | ||||||
Function / homology | ![]() mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase / mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity / carbohydrate metabolic process / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Rao, V. / Tao, C. / Guan, C. / Van Roey, P. | ||||||
![]() | ![]() Title: Mutations of endo-beta-N-acetylglucosaminidase H active site residues Assp130 and Glu132: activities and conformations. Authors: Rao, V. / Cui, T. / Guan, C. / Van Roey, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 115.1 KB | Display | ![]() |
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PDB format | ![]() | 89 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.8 KB | Display | ![]() |
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Full document | ![]() | 435 KB | Display | |
Data in XML | ![]() | 24.1 KB | Display | |
Data in CIF | ![]() | 35 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1c3fC ![]() 1c8xC ![]() 1c8yC ![]() 1c91C ![]() 1c92C ![]() 1c93C 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
#1: Protein | Mass: 28524.428 Da / Num. of mol.: 2 / Mutation: E132Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P04067, mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.76 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 19% PEG1000, 100 MM ZN(AC)2 100 MM CACODYLATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 1, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. all: 51615 / Num. obs: 27256 / % possible obs: 87.6 % / Observed criterion σ(F): 2 / Rmerge(I) obs: 0.066 |
Reflection shell | Resolution: 2.1→2.2 Å / % possible all: 83 |
Reflection | *PLUS % possible obs: 91 % / Redundancy: 3 % / Rmerge(I) obs: 0.076 |
Reflection shell | *PLUS % possible obs: 88 % |
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Processing
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Refinement | Resolution: 2.1→10 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.1→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 10 Å / σ(F): 2 / Rfactor obs: 0.212 / Rfactor Rwork: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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