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- PDB-2ok7: Ferredoxin-NADP+ reductase from Plasmodium falciparum with 2'P-AMP -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ok7 | ||||||
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Title | Ferredoxin-NADP+ reductase from Plasmodium falciparum with 2'P-AMP | ||||||
![]() | Putative ferredoxin--NADP reductase | ||||||
![]() | OXIDOREDUCTASE / disulfide-stabilized dimer | ||||||
Function / homology | ![]() ferredoxin-NAD(P) reductase activity / regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway / apicoplast / ferredoxin-NADP+ reductase / ferredoxin-NADP+ reductase activity / FAD binding / electron transfer activity / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Milani, M. / Mastrangelo, E. / Bolognesi, M. | ||||||
![]() | ![]() Title: Ferredoxin-NADP(+) Reductase from Plasmodium falciparum Undergoes NADP(+)-dependent Dimerization and Inactivation: Functional and Crystallographic Analysis. Authors: Milani, M. / Balconi, E. / Aliverti, A. / Mastrangelo, E. / Seeber, F. / Bolognesi, M. / 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 | ![]() | 332.7 KB | Display | ![]() |
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PDB format | ![]() | 268.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2ok8C ![]() 1jb9S 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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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 37315.988 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q6LF82, UniProt: C6KT68*PLUS, ferredoxin-NADP+ reductase #2: Chemical | ChemComp-NA / | #3: Chemical | ChemComp-FAD / #4: Chemical | ChemComp-A2P / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.96 % |
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Crystal grow | Temperature: 293 K / Method: microbatch / pH: 6 Details: PEG 4000 25%, buffer Na cacodylate, Na acetate 0.2 M, pH 6., microbatch, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 5, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.931 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→60 Å / Num. all: 61398 / Num. obs: 61398 / % possible obs: 98.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Rmerge(I) obs: 0.102 / Net I/σ(I): 9.8 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.476 / Mean I/σ(I) obs: 2.3 / Num. unique all: 8933 / % possible all: 98.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1jb9 Resolution: 2.7→30 Å / Cor.coef. Fo:Fc: 0.879 / Cor.coef. Fo:Fc free: 0.817 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 1.392 / ESU R Free: 0.429 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.137 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.77 Å / Total num. of bins used: 20
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