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- PDB-1h85: FERREDOXIN:NADP+ REDUCTASE MUTANT WITH VAL 136 REPLACED BY LEU (V136L) -
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Open data
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Basic information
Entry | Database: PDB / ID: 1h85 | ||||||
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Title | FERREDOXIN:NADP+ REDUCTASE MUTANT WITH VAL 136 REPLACED BY LEU (V136L) | ||||||
![]() | FERREDOXIN--NADP REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / FLAVOPROTEIN / NADP / ELECTRON TRANSPORT | ||||||
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 | ![]() ![]() | ||||||
![]() | Hermoso, J.A. / Mayoral, T. / Medina, M. / Sanz-Aparicio, J. / Gomez-Moreno, C. | ||||||
![]() | ![]() Title: Role of a Cluster of Hydrophobic Residues Near the Fad Cofactor in Anabaena Pcc 7119 Ferredoxin-Nadp+ Reductase for Optimal Complex Formation and Electron Transfer to Ferredoxin Authors: Marti-Nez-Julvez, M. / Nogues, I. / Faro, M. / Hurley, J.K. / Brodie, T.B. / Mayoral, T. / Sanz-Aparicio, J. / Hermoso, J.A. / Stankovich, M.T. / Medina, M. / Tollin, G. / Gomez-Moreno, C. #1: ![]() Title: X-Ray Structure of the Ferredoxin:Nadp+ Reductase from the Cyanobacterium Anabanena Pcc 7119 at 1.8 Angstroms Resolution, and Crystallographic Studies of Nadp Binding at 2.25 Angstroms Resolution Authors: Serre, L. / Vellieux, F.M.D. / Medina, M. / Gomez-Moreno, C. / Fontecilla, J.C. / Frey, M. #2: ![]() Title: Probing the Determinants of Coenzyme Specificity in Ferredoxin-Nadp+ Reductase by Site-Directed Mutagenesis Authors: Medina, M. / Luquita, A. / Tejero, J. / Hermoso, J. / Mayoral, T. / Sanz-Aparicio, J. / Grever, K. / Gomez-Moreno, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.3 KB | Display | ![]() |
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PDB format | ![]() | 57.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 473.8 KB | Display | ![]() |
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Full document | ![]() | 477.1 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 13.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1qgzC ![]() 1qh0C ![]() 1queS 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: 33216.734 Da / Num. of mol.: 1 / 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: Water | ChemComp-HOH / |
Compound details | CHAIN A ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 60 % |
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Crystal grow | pH: 5 / Details: pH 5.00 |
-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 15, 2000 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→37.5 Å / Num. obs: 18325 / % possible obs: 99.4 % / Redundancy: 12.6 % / Rmerge(I) obs: 0.1 / Rsym value: 0.1 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 10.7 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 3.1 / Rsym value: 0.26 / % possible all: 96.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1QUE Resolution: 2.3→10 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: FREE R-VALUE / σ(F): 0
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Displacement parameters | Biso mean: 7.08 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.4 Å / Total num. of bins used: 8
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