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- PDB-6qun: Crystal structure of AtGapC1 with the catalytic Cys149 irreversib... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6qun | ||||||
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Title | Crystal structure of AtGapC1 with the catalytic Cys149 irreversibly oxidized by H2O2 treatment | ||||||
![]() | Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic | ||||||
![]() | OXIDOREDUCTASE / Rossman fold / NAD binding / Glycolytic process / oxidative stress / Hydrogen peroxide | ||||||
Function / homology | ![]() fruit development / glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity / seed development / salicylic acid binding / response to sucrose / glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) / apoplast / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / mitochondrial envelope / plant-type vacuole ...fruit development / glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity / seed development / salicylic acid binding / response to sucrose / glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) / apoplast / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / mitochondrial envelope / plant-type vacuole / response to redox state / chloroplast / gluconeogenesis / glycolytic process / response to hydrogen peroxide / NAD binding / NADP binding / response to heat / response to oxidative stress / copper ion binding / positive regulation of DNA-templated transcription / mitochondrion / DNA binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fermani, S. / Zaffagnini, M. / Falini, G. / Trost, P. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Glutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates. Authors: Zaffagnini, M. / Marchand, C.H. / Malferrari, M. / Murail, S. / Bonacchi, S. / Genovese, D. / Montalti, M. / Venturoli, G. / Falini, G. / Baaden, M. / Lemaire, S.D. / Fermani, S. / Trost, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 277.8 KB | Display | ![]() |
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PDB format | ![]() | 229.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6quqC ![]() 4z0hS 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 on special symmetry positions |
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Components
#1: Protein | Mass: 36549.707 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: The catalytic cysteine is oxidated to sulphinic acid Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P25858, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) #2: Chemical | #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.43 Å3/Da / Density % sol: 49.31 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 3.0 M (NH4)2SO4, 0.1 M Hepes-NaOH (pH 7.5), 0.1 mM H2O2 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: May 15, 2012 Details: Cilindrical Mirror with 50 nm Pt-coating, oridal Mirros with 50 nm Pt-coating |
Radiation | Monochromator: Si 111 double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.26 Å / Relative weight: 1 |
Reflection | Resolution: 3→47.79 Å / Num. obs: 15798 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 7.8 % / Biso Wilson estimate: 62.2 Å2 / Rmerge(I) obs: 0.112 / Rpim(I) all: 0.043 / Rrim(I) all: 0.12 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 8.1 % / Rmerge(I) obs: 0.453 / Mean I/σ(I) obs: 4.1 / Num. unique obs: 2164 / Rpim(I) all: 0.168 / Rrim(I) all: 0.483 / % possible all: 98.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4Z0H Resolution: 3→47.785 Å / SU ML: 0.47 / Cross valid method: FREE R-VALUE / Phase error: 29.72
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 72.9 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→47.785 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 38.4077 Å / Origin y: 37.11 Å / Origin z: 236.3742 Å
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Refinement TLS group | Selection details: (chain O and resseq 0:337) or (chain R and resseq 0:337) |