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Open data
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Basic information
Entry | Database: PDB / ID: 1lwh | ||||||
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Title | CRYSTAL STRUCTURE OF T. MARITIMA 4-ALPHA-GLUCANOTRANSFERASE | ||||||
![]() | 4-alpha-glucanotransferase | ||||||
![]() | TRANSFERASE / 4-alpha-glucanotransferase / alpha-amylase family / Thermotoga maritima / acarbose | ||||||
Function / homology | ![]() 4-alpha-glucanotransferase / 4-alpha-glucanotransferase activity / : / glucan 1,4-alpha-maltotriohydrolase activity / oligo-1,6-glucosidase activity / maltose catabolic process / : / sucrose alpha-glucosidase activity / sucrose catabolic process / oligosaccharide catabolic process ...4-alpha-glucanotransferase / 4-alpha-glucanotransferase activity / : / glucan 1,4-alpha-maltotriohydrolase activity / oligo-1,6-glucosidase activity / maltose catabolic process / : / sucrose alpha-glucosidase activity / sucrose catabolic process / oligosaccharide catabolic process / alpha-amylase activity / amino acid transport / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Roujeinikova, A. / Raasch, C. / Sedelnikova, S. / Liebl, W. / Rice, D.W. | ||||||
![]() | ![]() Title: CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA 4-ALPHA-GLUCANOTRANSFERASE AND ITS ACARBOSE COMPLEX: IMPLICATIONS FOR SUBSTRATE SPECIFICITY AND CATALYSIS Authors: Roujeinikova, A. / Raasch, C. / Sedelnikova, S. / Liebl, W. / Rice, D.W. #1: ![]() Title: CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC STUDIES ON 4-ALPHA-GLUCANOTRANSFERASE FROM THERMOTOGA MARITIMA Authors: Roujeinikova, A. / Raasch, C. / Sedelnikova, S. / Liebl, W. / Rice, D.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 178.1 KB | Display | ![]() |
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PDB format | ![]() | 142 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 377.8 KB | Display | ![]() |
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Full document | ![]() | 402.2 KB | Display | |
Data in XML | ![]() | 20.8 KB | Display | |
Data in CIF | ![]() | 31.9 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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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | The dimer in the asymmetric unit is the biological unit |
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Components
#1: Protein | Mass: 51925.898 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4 Å3/Da / Density % sol: 69.25 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 26-29% PEG 5000, 200-300 mM Ammonium Sulphate, 3 mM CaCl2, 80 mM MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusionDetails: Roujeinikova, A., (2001) Acta Crystallogr., Sect.D, 57, 1046. | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Sep 7, 2000 |
Radiation | Monochromator: triangular single crystal Si monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→100 Å / Num. obs: 45954 / % possible obs: 89 % / Observed criterion σ(I): -3 / Redundancy: 5.4 % / Biso Wilson estimate: 55 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 22.5 |
Reflection shell | Resolution: 2.6→2.66 Å / Redundancy: 1.5 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 2.5 / Num. unique all: 2151 / % possible all: 63 |
Reflection | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 100 Å / % possible obs: 89 % / Num. measured all: 247046 / Rmerge(I) obs: 0.05 |
Reflection shell | *PLUS % possible obs: 63 % / Rmerge(I) obs: 0.36 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.6→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 10 Å / Rfactor Rfree: 0.278 / Rfactor Rwork: 0.224 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_bond_d / Dev ideal: 0.01 |