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- PDB-1xh2: Structure of the N298S variant of human pancreatic alpha-amylase ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xh2 | |||||||||
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Title | Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose | |||||||||
![]() | Alpha-amylase, pancreatic | |||||||||
![]() | HYDROLASE / Chloride Amylase Enzyme Acarbose / Inhibitor | |||||||||
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 | ![]() ![]() | |||||||||
![]() | Maurus, R. / Begum, A. / Kuo, H.H. / Racaza, A. / Numao, S. / Overall, C.M. / Withers, S.G. / Brayer, G.D. | |||||||||
![]() | ![]() Title: Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase Authors: Maurus, R. / Begum, A. / Kuo, H.H. / Racaza, A. / Numao, S. / Andersen, C. / Tams, J.W. / Vind, J. / Overall, C.M. / Withers, S.G. / Brayer, G.D. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.6 KB | Display | ![]() |
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PDB format | ![]() | 91.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 498 KB | Display | ![]() |
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Full document | ![]() | 506 KB | Display | |
Data in XML | ![]() | 12.5 KB | Display | |
Data in CIF | ![]() | 20 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1xgzC ![]() 1xh0C ![]() 1xh1C ![]() 1bsiS 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 55904.281 Da / Num. of mol.: 1 / Mutation: N298S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Sugars , 2 types, 2 molecules ![](data/chem/img/NAG.gif)
![](data/chem/img/ARE.gif)
![](data/chem/img/ARE.gif)
#2: Sugar | ChemComp-NAG / |
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#3: Sugar | ChemComp-ARE / |
-Non-polymers , 3 types, 317 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-CA / |
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#5: Chemical | ChemComp-CL / |
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.68 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: MPD, cacodylate , pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 24, 2003 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→25 Å / Num. obs: 25669 / % possible obs: 97 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 16.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1BSI Resolution: 2.2→10 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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