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- PDB-1tmq: STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WIT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tmq | |||||||||
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Title | STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR | |||||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / ALPHA-AMYLASE / CARBOHYDRATE METABOLISM / ALPHA-1 / 4-GLUCAN-4-GLUCANOHYDROLASE / HYDROLASE BIFUNCTIONAL ALPHA-AMYLASE/TRYPSIN INHIBITOR / COMPLEX (ENZYME- INHIBITOR) / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | |||||||||
Function / homology | ![]() alpha-amylase inhibitor activity / alpha-amylase / carbohydrate catabolic process / alpha-amylase activity / chloride ion binding / serine-type endopeptidase inhibitor activity / calcium ion binding / extracellular space / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Gomis-Rueth, F.X. / Strobl, S. / Glockshuber, R. | |||||||||
![]() | ![]() Title: A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution. Authors: Strobl, S. / Maskos, K. / Wiegand, G. / Huber, R. / Gomis-Ruth, F.X. / Glockshuber, R. #1: ![]() Title: The Alpha-Amylase from the Yellow Meal Worm: Complete Primary Structure, Crystallization and Preliminary X-Ray Analysis Authors: Strobl, S. / Gomis-Ruth, F.X. / Maskos, K. / Frank, G. / Huber, R. / Glockshuber, R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 132.3 KB | Display | ![]() |
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PDB format | ![]() | 101.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 377.1 KB | Display | ![]() |
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Full document | ![]() | 385.8 KB | Display | |
Data in XML | ![]() | 13.4 KB | Display | |
Data in CIF | ![]() | 22 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bipS 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
#1: Protein | Mass: 51263.066 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Protein | Mass: 12715.823 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#3: Chemical | ChemComp-CL / |
#4: Chemical | ChemComp-CA / |
#5: Water | ChemComp-HOH / |
Compound details | THE ALPHA-AMYLASE N-TERMINUS BLOCKS AGAINST AMINOPEPTIDASE ACTIVITY BY GLUTAMINE CYCLIZATION TO ...THE ALPHA-AMYLASE N-TERMINUS BLOCKS AGAINST AMINOPEPTI |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.83 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Details: 200MM AMMONIUM PHOSPHATE, 100MM TRIS-HCL, PH 8.5, 50% (W/V) 2-METHYL-2,4- PENTANEDIOL | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 5.4 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromator: GRAPHITE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 28178 / % possible obs: 97.3 % / Observed criterion σ(I): 3 / Redundancy: 2.8 % / Rmerge(I) obs: 0.093 / Net I/σ(I): 5.5 |
Reflection shell | Resolution: 2.5→2.56 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.284 / Mean I/σ(I) obs: 2.5 / % possible all: 89.8 |
Reflection | *PLUS Observed criterion σ(I): 3 / Num. measured all: 78106 |
Reflection shell | *PLUS % possible obs: 89.8 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1BIP Resolution: 2.5→7 Å / Cross valid method: FREE R FACTOR / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.5→7 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 7 Å / σ(F): 0 / % reflection Rfree: 7 % | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||
Refine LS restraints | *PLUS
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