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- PDB-1bx1: FERREDOXIN:NADP+ OXIDOREDUCTASE (FERREDOXIN REDUCTASE) MUTANT E312Q -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bx1 | ||||||
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Title | FERREDOXIN:NADP+ OXIDOREDUCTASE (FERREDOXIN REDUCTASE) MUTANT E312Q | ||||||
![]() | PROTEIN (FERREDOXIN:NADP+ OXIDOREDUCTASE) | ||||||
![]() | OXIDOREDUCTASE / FLAVOPROTEIN | ||||||
Function / homology | ![]() chloroplast thylakoid membrane protein complex / ferredoxin-NADP+ reductase / ferredoxin-NADP+ reductase activity / NADPH dehydrogenase activity / chloroplast stroma / photosynthesis / electron transport chain Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Aliverti, A. / Deng, Z. / Ravasi, D. / Piubelli, L. / Karplus, P.A. / Zanetti, G. | ||||||
![]() | ![]() Title: Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase. Authors: Aliverti, A. / Deng, Z. / Ravasi, D. / Piubelli, L. / Karplus, P.A. / Zanetti, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 79.7 KB | Display | ![]() |
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PDB format | ![]() | 57.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 769.7 KB | Display | ![]() |
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Full document | ![]() | 772.4 KB | Display | |
Data in XML | ![]() | 15.6 KB | Display | |
Data in CIF | ![]() | 22.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bx0C ![]() 1frqC ![]() 1fnbS 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: 35428.758 Da / Num. of mol.: 1 / Mutation: E312Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-SO4 / |
#4: Chemical | ChemComp-FAD / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 49 % | ||||||||||||||||||
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Crystal grow | pH: 4.5 / Details: pH 4.5 | ||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging dropDetails: drop is produced by a 1:1(v/v) mixture of the stored FNR stock with a reservoir | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: SDMS / Detector: AREA DETECTOR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→25 Å / Num. obs: 27319 / % possible obs: 98.8 % / Redundancy: 2.7 % / Rsym value: 0.086 / Net I/σ(I): 11.7 |
Reflection shell | Resolution: 1.9→1.94 Å / Mean I/σ(I) obs: 2.7 / Rsym value: 0.291 / % possible all: 93.1 |
Reflection | *PLUS Num. measured all: 74220 / Rmerge(I) obs: 0.086 |
Reflection shell | *PLUS % possible obs: 93.1 % / Rmerge(I) obs: 0.291 |
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Processing
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Refinement | Method to determine structure: OTHER Starting model: PDB ENTRY 1FNB Resolution: 1.9→10 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / σ(F): 0
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Displacement parameters | Biso mean: 18.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.99 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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