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- PDB-1cru: SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CAL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cru | ||||||
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Title | SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE | ||||||
![]() | PROTEIN (SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE) | ||||||
![]() | OXIDOREDUCTASE / BETA-PROPELLER / SUPERBARREL / COMPLEX WITH THE COFACTOR PQQ AND THE INHIBITOR METHYLHYDRAZINE | ||||||
Function / homology | ![]() glucose 1-dehydrogenase (PQQ, quinone) / quinoprotein glucose dehydrogenase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Oubrie, A. / Rozeboom, H.J. / Dijkstra, B.W. | ||||||
![]() | ![]() Title: Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex. Authors: Oubrie, A. / Rozeboom, H.J. / Dijkstra, B.W. #1: ![]() Title: The 1.7 Angstrom Crystal Structure of the Apo-Form of the Soluble Quinoprotein Glucose Dehydrogenase from Acinetobacter Calcoaceticus Reveals a Novel Internal Sequence Repeat Authors: Oubrie, A. / Rozeboom, H.J. / Kalk, K.H. / Duine, J.A. / Dijkstra, B.W. #2: ![]() Title: Structure and Mechanism of Soluble Quinoprotein Glucose Dehydrogenase Authors: Oubrie, A. / Rozeboom, H.J. / Kalk, K.H. / Olsthoorn, A.J.J. / Duine, J.A. / Dijsktra, B.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 | ![]() | 204.8 KB | Display | ![]() |
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PDB format | ![]() | 167.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 42.6 KB | Display | |
Data in CIF | ![]() | 64.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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, 2 molecules AB
#1: Protein | Mass: 50293.207 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 5 types, 902 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/PQQ.gif)
![](data/chem/img/HDN.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PQQ.gif)
![](data/chem/img/HDN.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-CA / #3: Chemical | #4: Chemical | #5: Chemical | ChemComp-GOL / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.64 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9.2 Details: PEG 6000, SODIUM CHLORIDE, CALCIUM CHLORIDE, TRIS, GLYCINE, pH 9.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / Details: Oubrie, A., (1999) J.Mol.Biol., 289, 319. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: MARRESEARCH / Detector: CCD / Date: Apr 5, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9475 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→100 Å / Num. obs: 142076 / % possible obs: 97.8 % / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Biso Wilson estimate: 16.8 Å2 / Rmerge(I) obs: 0.034 / Net I/σ(I): 30.2 |
Reflection shell | Resolution: 1.5→1.53 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.34 / % possible all: 91.2 |
Reflection | *PLUS Num. measured all: 580379 |
Reflection shell | *PLUS % possible obs: 91.2 % |
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Processing
Software |
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Refinement | Resolution: 1.5→20 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.5→20 Å
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Software | *PLUS Name: 'REFMAC+X-PLOR3.843' / Classification: refinement | ||||||||||||||||||||||||
Refine LS restraints | *PLUS
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