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- PDB-1jdd: MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE COCRYSTALLIZED W... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1jdd | |||||||||
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Title | MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE COCRYSTALLIZED WITH MALTOTETRAOSE (CRYSTAL TYPE 2) | |||||||||
![]() | 1,4-ALPHA MALTOTETRAHYDROLASE | |||||||||
![]() | HYDROLASE / MALTOTETRAOSE-FORMING EXO AMYLASE | |||||||||
Function / homology | ![]() glucan 1,4-alpha-maltotetraohydrolase / glucan 1,4-alpha-maltotetraohydrolase activity / starch catabolic process / starch binding / alpha-amylase activity / extracellular space / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Yoshioka, Y. / Hasegawa, K. / Matsuura, Y. / Katsube, Y. / Kubota, M. | |||||||||
![]() | ![]() Title: Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose. Authors: Yoshioka, Y. / Hasegawa, K. / Matsuura, Y. / Katsube, Y. / Kubota, M. #1: ![]() Title: Crystal Structure of a Maltotetraose-Forming Exo-Amylase from Pseudomonas Stutzeri Authors: Morishita, Y. / Hasegawa, K. / Matsuura, Y. / Katsube, Y. / Kubota, M. / Sakai, S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 96.2 KB | Display | ![]() |
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PDB format | ![]() | 76.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 727.7 KB | Display | ![]() |
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Full document | ![]() | 746.6 KB | Display | |
Data in XML | ![]() | 20.8 KB | Display | |
Data in CIF | ![]() | 29.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 47408.637 Da / Num. of mol.: 1 / Mutation: E219Q Source method: isolated from a genetically manipulated source Details: CRYSTAL TYPE 2 / Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P13507, glucan 1,4-alpha-maltotetraohydrolase | ||
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#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltotetraose | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 56 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Nov 27, 1992 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 35190 / % possible obs: 84.6 % / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.089 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. measured all: 102610 |
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Processing
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Refinement | Resolution: 1.9→10 Å / σ(F): 2 / Details: X-PLOR WAS ALSO USED. /
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Refine analyze | Luzzati coordinate error obs: 0.18 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.191 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |