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- PDB-1pig: PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532 -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pig | ||||||||||||
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Title | PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532 | ||||||||||||
![]() | ALPHA-AMYLASE | ||||||||||||
![]() | GLYCOSYLTRANSFERASE / ALPHA-AMYLASE ALPHA-1 / 4-GLUCAN-4-GLUCANOHYDROLASE GLYCOSYLTRANSFERASE | ||||||||||||
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 | ![]() | ||||||||||||
![]() | Machius, M. / Vertesy, L. / Huber, R. / Wiegand, G. | ||||||||||||
![]() | ![]() Title: Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics. Authors: Machius, M. / Vertesy, L. / Huber, R. / Wiegand, G. #1: ![]() Title: The Crystal Structure of Porcine Pancreatic Alpha-Amylase in Complex with the Microbial Inhibitor Tendamistat Authors: Wiegand, G. / Epp, O. / Huber, R. #2: ![]() Title: Carbohydrate Binding Sites in a Pancreatic Alpha-Amylase-Substrate Complex, Derived from X-Ray Structure Analysis at 2.1 Angstrom Resolution Authors: Qian, M. / Haser, R. / Payan, F. #3: ![]() Title: Refined Molecular Structure of Pig Pancreatic Alpha-Amylase at 2.1 A Resolution Authors: Larson, S.B. / Greenwood, A. / Cascio, D. / Day, J. / McPherson, A. #4: ![]() 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. #5: ![]() Title: Structure and Molecular Model Refinement of Pig Pancreatic Alpha-Amylase at 2.1 A 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 | ![]() | 114.9 KB | Display | ![]() |
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PDB format | ![]() | 90.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 639.3 KB | Display | ![]() |
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Full document | ![]() | 643.6 KB | Display | |
Data in XML | ![]() | 12.1 KB | Display | |
Data in CIF | ![]() | 19.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1pifSC 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 55373.680 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Sugars , 5 types, 5 molecules ![](data/chem/img/BGC.gif)
#2: Polysaccharide | 4-amino-4,6-dideoxy-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#3: Polysaccharide | 4-amino-4,6-dideoxy-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#4: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose |
#5: Polysaccharide | beta-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-cellobiose |
#7: Sugar | ChemComp-BGC / |
-Non-polymers , 4 types, 231 molecules ![](data/chem/img/HMC.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
#6: Chemical | ChemComp-HMC / |
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#8: Chemical | ChemComp-CA / |
#9: Chemical | ChemComp-CL / |
#10: Water | ChemComp-HOH / |
-Details
Nonpolymer details | TRESTATIN LIKE COMPOUNDS HAVE BEEN ISOLATED FROM STREPTOMYCES GALBUS CULTURE MEDIUM AND TREATED ...TRESTATIN LIKE COMPOUNDS HAVE BEEN ISOLATED FROM STREPTOMYC |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.39 Å3/Da / Density % sol: 72 % | ||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion / pH: 6 Details: VAPOR DIFFUSION; 10 MICROLITER OF PROTEIN (15 MG/ML IN 0.1 M AMMONIUM CACODYLATE, PH 10.0 0.001 M V-1532) WERE STEPWISE CONCENTRATED OVER 0.1, 0.15, AND 0.25 M AMMONIUM CACODYLATE, PH 6.0., vapor diffusion PH range: 6.0-10.0 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 275 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 20, 1995 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20.5 Å / Num. obs: 47260 / % possible obs: 93.7 % / Observed criterion σ(I): 2 / Redundancy: 4.1 % / Biso Wilson estimate: 32.1 Å2 / Rmerge(I) obs: 0.123 |
Reflection shell | Resolution: 2.2→2.3 Å / % possible all: 97.8 |
Reflection shell | *PLUS % possible obs: 97.8 % |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: 1PIF Resolution: 2.2→7 Å / σ(F): 2
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Displacement parameters | Biso mean: 28.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.3 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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