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- PDB-1kb3: Three Dimensional Structure Analysis of the R195A Variant of Huma... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1kb3 | |||||||||
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Title | Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase | |||||||||
![]() | ALPHA-AMYLASE, PANCREATIC | |||||||||
![]() | HYDROLASE / alpha-amylase / chloride binding / PICHIA PASTORIS / MUTAGENESIS / CATALYSIS / PANCREATIC / ENZYME / HUMAN | |||||||||
Function / homology | ![]() polysaccharide digestion / Digestion of dietary carbohydrate / alpha-amylase / carbohydrate catabolic process / alpha-amylase activity / chloride ion binding / carbohydrate metabolic process / calcium ion binding / extracellular space / extracellular exosome / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Numao, S. / Maurus, R. / Sidhu, G. / Wang, Y. / Overall, C.M. / Brayer, G.D. / Withers, S.G. | |||||||||
![]() | ![]() Title: Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase. Authors: Numao, S. / Maurus, R. / Sidhu, G. / Wang, Y. / Overall, C.M. / Brayer, G.D. / Withers, S.G. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 116.5 KB | Display | ![]() |
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PDB format | ![]() | 87.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 392.7 KB | Display | ![]() |
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Full document | ![]() | 401.3 KB | Display | |
Data in XML | ![]() | 12.2 KB | Display | |
Data in CIF | ![]() | 18.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1kguC ![]() 1kgwC ![]() 1kgxC ![]() 1bsiS 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: 55845.188 Da / Num. of mol.: 1 / Mutation: R195A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Sugar | ChemComp-NAG / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.89 % |
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Crystal grow | Method: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jul 7, 1999 / Details: mirrors |
Radiation | Monochromator: mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→30 Å / Num. all: 41336 / Num. obs: 41336 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Rmerge(I) obs: 0.046 / Net I/σ(I): 18.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1BSI Resolution: 2.1→10 Å / Isotropic thermal model: Isotropic / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 17.1 Å2 | ||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.22 Å | ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→10 Å
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