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- PDB-1uxu: Structural basis for allosteric regulation and substrate specific... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1uxu | ||||||
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Title | Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Thermoproteus tenax | ||||||
![]() | GLYCERALDEHYDE-3- ... | ||||||
![]() | OXIDOREDUCTASE / GAPN / ALDH / AMP / GLYCERALDEHYDE 3-PHOSPHATE / GLYCOLYSIS / REGULATION / CATALYSIS | ||||||
Function / homology | ![]() glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] / glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity / lactaldehyde dehydrogenase (NAD+) activity / metabolic process / NAD binding / NADP binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lorentzen, E. / Hensel, R. / Pohl, E. | ||||||
![]() | ![]() Title: Structural Basis of Allosteric Regulation and Substrate Specificity of the Non-Phosphorylating Glyceraldehyde 3-Phosphate Dehydrogenase from Thermoproteus Tenax Authors: Lorentzen, E. / Hensel, R. / Knura, T. / Ahmed, H. / Pohl, E. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 118.1 KB | Display | ![]() |
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PDB format | ![]() | 89.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 24.8 KB | Display | |
Data in CIF | ![]() | 35.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1uxnC ![]() 1uxpC ![]() 1uxqC ![]() 1uxrC ![]() 1uxtC ![]() 1uxvC ![]() 1ky8S 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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1 | ![]()
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Unit cell |
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Components
-GLYCERALDEHYDE-3- ... , 1 types, 1 molecules A
#1: Protein | Mass: 54218.367 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Details: GLYCERALDEHYDE 3-PHOSPHATE, AMP AND NADP(H) BOUND NONCOVALENTLY Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: O57693, glyceraldehyde-3-phosphate dehydrogenase (NADP+) |
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-Non-polymers , 5 types, 291 molecules ![](data/chem/img/NAP.gif)
![](data/chem/img/AMP.gif)
![](data/chem/img/G3H.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/AMP.gif)
![](data/chem/img/G3H.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-NAP / |
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#3: Chemical | ChemComp-AMP / |
#4: Chemical | ChemComp-G3H / |
#5: Chemical | ChemComp-NA / |
#6: Water | ChemComp-HOH / |
-Details
Compound details | ENGINEEREDSequence details | SER 402 LEU IS DUE TO A SEQUENCING | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 6 Å3/Da / Density % sol: 80 % |
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Crystal grow | pH: 5.6 Details: 2M SODIUM FORMATE PH 5.6, 0.1 M SODIUM ACETATE PH 5.6, 50 MM AMP, 1 MM GLYCERALDEHYDE 3-PHOSPHATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Aug 15, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8453 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→30 Å / Num. obs: 58447 / % possible obs: 92 % / Redundancy: 13 % / Biso Wilson estimate: 51 Å2 / Rmerge(I) obs: 0.049 / Net I/σ(I): 28 |
Reflection shell | Resolution: 2.25→2.35 Å / Redundancy: 13 % / Rmerge(I) obs: 0.37 / Mean I/σ(I) obs: 5 / % possible all: 94 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1KY8 Resolution: 2.25→30 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: RESIDUES 1-2 NOT MODELED, RESIDUES 499-501 AS ALANINES
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Displacement parameters | Biso mean: 56 Å2
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Refinement step | Cycle: LAST / Resolution: 2.25→30 Å
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Refine LS restraints |
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