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- PDB-1ppi: THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ppi | |||||||||
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Title | THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION | |||||||||
![]() | ALPHA-AMYLASE | |||||||||
![]() | HYDROLASE (O-GLYCOSYL) | |||||||||
Function / homology | ![]() alpha-amylase / carbohydrate catabolic process / alpha-amylase activity / chloride ion binding / carbohydrate metabolic process / calcium ion binding / extracellular space Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Qian, M. / Haser, R. / Payan, F. | |||||||||
![]() | ![]() Title: The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution. Authors: Qian, M. / Haser, R. / Buisson, G. / Duee, E. / Payan, F. #1: ![]() Title: Structure and Molecular Model Refinement of Pig Pancreatic Alpha-Amylase at 2.1 Angstroms Resolution Authors: Qian, M. / Haser, R. / Payan, F. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 118.6 KB | Display | ![]() |
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PDB format | ![]() | 92.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 497.5 KB | Display | ![]() |
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Full document | ![]() | 511.6 KB | Display | |
Data in XML | ![]() | 12.9 KB | Display | |
Data in CIF | ![]() | 21.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: CIS PROLINE - PRO 54 / 2: CIS PROLINE - PRO 130 3: CALCIUM BINDING SITE. CHLORIDE BINDING SITE. AMYLASE -CARBOHYDRATES INTERACTION IN ACTIVE SITE. |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 55435.766 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Sugars , 2 types, 2 molecules
#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose |
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#3: Polysaccharide | 4,6-dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5- ...4,6-dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5-enopyranose-(1-4)-beta-D-glucopyranose Type: oligosaccharide / Mass: 477.417 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
-Non-polymers , 3 types, 395 molecules ![](data/chem/img/CL.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-CL / |
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#5: Chemical | ChemComp-CA / |
#6: Water | ChemComp-HOH / |
-Details
Nonpolymer details | ACARBOSE IS A PSEUDOSACCHARRIDE THAT IS ACTED ON BY THE ENZYME. THIS YIELDS A FIVE-UNIT PRODUCT ...ACARBOSE IS A PSEUDOSACC |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.62 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.06 Å / Num. obs: 29212 / % possible obs: 95 % / Num. measured all: 93924 / Rmerge(I) obs: 0.036 |
Reflection shell | *PLUS Mean I/σ(I) obs: 9.9 |
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Processing
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Refinement | Resolution: 2.2→8 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |