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- PDB-2vyq: FERREDOXIN:NADP REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, AL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2vyq | ||||||
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Title | FERREDOXIN:NADP REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR, LEU 263 REPLACED BY PRO AND TYR 303 REPLACED BY SER (T155G-A160T-L263P-Y303S) | ||||||
![]() | FERREDOXIN-NADP REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / PHYCOBILISOME / FAD / NADP / MEMBRANE / THYLAKOID / FLAVOPROTEIN | ||||||
Function / homology | ![]() ferredoxin-NADP+ reductase / ferredoxin-NADP+ reductase activity / NADPH dehydrogenase activity / phycobilisome / plasma membrane-derived thylakoid membrane / electron transport chain / NADP binding / flavin adenine dinucleotide binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Herguedas, B. / Martinez-Julvez, M. / Hermoso, J.A. / Peregrina, J.R. / Medina, M. | ||||||
![]() | ![]() Title: Protein Motifs Involved in Coenzyme Interaction and Enzymatic Efficiency in Anabaena Ferredoxin-Nadp+ Reductase. Authors: Peregrina, J.R. / Herguedas, B. / Hermoso, J.A. / Martinez-Julvez, M. / Medina, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 87.3 KB | Display | ![]() |
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PDB format | ![]() | 64.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 727 KB | Display | ![]() |
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Full document | ![]() | 728.2 KB | Display | |
Data in XML | ![]() | 15.1 KB | Display | |
Data in CIF | ![]() | 26.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2bmwC ![]() 2vzlC ![]() 1queS C: citing same article ( S: Starting model for refinement |
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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: 34067.691 Da / Num. of mol.: 1 / Fragment: RESIDUES 137-440 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||||
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#2: Chemical | ChemComp-FAD / | ||||||
#3: Chemical | ChemComp-SO4 / | ||||||
#4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, THR 292 TO GLY ENGINEERED RESIDUE IN CHAIN A, ALA 297 TO THR ...ENGINEERED | Sequence details | FNR MUTANT (T155G, A160T, L263P, Y303S) | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.9 % / Description: NONE |
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Crystal grow | pH: 5.5 Details: 18-20 % (W/V) PEG 6000 20 MM AMMONIUM SULPHATE 0.1M MES/NAOH, PH 5.0-5.5 B-OCTYL GLYCOSIDE AT 2%(W/V) |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() |
Detector | Type: BRUKER-NONIUS / Detector: CCD / Date: Jun 30, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→75.38 Å / Num. obs: 30845 / % possible obs: 99.1 % / Observed criterion σ(I): 2 / Redundancy: 5.26 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 23.85 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 2.54 % / Rmerge(I) obs: 0.19 / Mean I/σ(I) obs: 5.45 / % possible all: 93.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1QUE Resolution: 1.9→19.8 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.935 / SU B: 2.282 / SU ML: 0.069 / Cross valid method: THROUGHOUT / ESU R: 0.124 / ESU R Free: 0.112 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES N237, M266 AND E301 PRESENTED DOUBLE CONFORMATION. OCCUPANCIES 0.5
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 12.18 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→19.8 Å
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Refine LS restraints |
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