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- PDB-1nqa: Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Repl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1nqa | ||||||
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Title | Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ala Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate | ||||||
![]() | Glyceraldehyde 3-phosphate dehydrogenase | ||||||
![]() | OXIDOREDUCTASE / Glycolysis / NAD | ||||||
Function / homology | ![]() glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / glycolytic process / glucose metabolic process / NAD binding / NADP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Didierjean, C. / Corbier, C. / Fatih, M. / Favier, F. / Boschi-Muller, S. / Branlant, G. / Aubry, A. | ||||||
![]() | ![]() Title: Crystal structure of two ternary complexes of phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus with NAD and D-Glyceraldehyde-3-Phosphate Authors: Didierjean, C. / Corbier, C. / Fatih, M. / Favier, F. / Boschi-Muller, S. / Branlant, G. / Aubry, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 277.6 KB | Display | ![]() |
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PDB format | ![]() | 223.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 57.9 KB | Display | |
Data in CIF | ![]() | 80.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1nptSC ![]() 1nq5C ![]() 1nqoC 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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Unit cell |
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Components
#1: Protein | Mass: 35958.984 Da / Num. of mol.: 4 / Mutation: C149A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: GAP / Plasmid: pBluescriptII / Production host: ![]() ![]() References: UniProt: P00362, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) #2: Chemical | ChemComp-NAD / #3: Chemical | ChemComp-G3H / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.61 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: PEG 4000, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: MAC Science DIP-2030B / Detector: IMAGE PLATE / Date: May 21, 1998 / Details: MIRRORS |
Radiation | Monochromator: Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→15 Å / Num. all: 86696 / Num. obs: 86696 / % possible obs: 96.3 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.065 / Net I/σ(I): 13.3 |
Reflection shell | Resolution: 2.2→2.28 Å / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 3.7 / % possible all: 98.9 |
Reflection | *PLUS Num. obs: 83284 |
Reflection shell | *PLUS % possible obs: 98.9 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1NPT Resolution: 2.2→8 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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LS refinement shell | Resolution: 2.2→2.28 Å
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Refinement | *PLUS % reflection Rfree: 10 % / Rfactor Rwork: 0.18 | ||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||
Refine LS restraints | *PLUS
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