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- PDB-1que: X-RAY STRUCTURE OF THE FERREDOXIN:NADP+ REDUCTASE FROM THE CYANOB... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1que | ||||||
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Title | X-RAY STRUCTURE OF THE FERREDOXIN:NADP+ REDUCTASE FROM THE CYANOBACTERIUM ANABAENA PCC 7119 AT 1.8 ANGSTROMS | ||||||
![]() | FERREDOXIN--NADP+ REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / FLAVOPROTEIN / NADP / FAD / THYLAKOID MEMBRANE / HYCOBILISOME / FNR / NADP+ REDUCTASE | ||||||
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 | ![]() ![]() | ||||||
![]() | Serre, L. / Frey, M. / Vellieux, F.M.D. | ||||||
![]() | ![]() Title: X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP+ binding at 2.25 A resolution. Authors: Serre, L. / Vellieux, F.M. / Medina, M. / Gomez-Moreno, C. / Fontecilla-Camps, J.C. / Frey, M. #1: ![]() Title: Crystals of Anabaena Pcc 7119 Ferredoxin-Nadp+ Reductase Authors: Serre, L. / Medina, M. / Gomez-Moreno, C. / Fontecilla-Camps, J.C. / Frey, M. #2: ![]() Title: Sequence of the Ferredoxin-Nadp(+)-Reductase Gene from Anabaena Pcc 7119 Authors: Fillat, M.F. / Bakker, H.A. / Weisbeek, P.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83 KB | Display | ![]() |
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PDB format | ![]() | 61.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 473.6 KB | Display | ![]() |
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Full document | ![]() | 476.8 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 13.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 34041.676 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-FAD / |
#4: Water | ChemComp-HOH / |
-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 | Method: vapor diffusion, hanging drop / pH: 7 Details: SEE REFERENCE 1., pH 7.0, vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Oct 1, 1992 |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 20337 / % possible obs: 85 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Rsym value: 0.07 |
Reflection shell | Resolution: 2.1→2.2 Å / Redundancy: 3 % / % possible all: 34 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 96286 / Rmerge(I) obs: 0.07 |
Reflection shell | *PLUS % possible obs: 34 % |
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Processing
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Refinement | Method to determine structure: ![]() Details: THE INITIAL MODEL WAS BUILT IN A M.I.R SOLVENT FLATTENED ELECTRON DENSITY MAP AT 2.6 ANGSTROMS RESOLUTION WITH THE SPINACH FNR MODEL AS A GUIDE (KARPLUS, DANIELS, HERRIOTT, SCIENCE 1991, 251 ...Details: THE INITIAL MODEL WAS BUILT IN A M.I.R SOLVENT FLATTENED ELECTRON DENSITY MAP AT 2.6 ANGSTROMS RESOLUTION WITH THE SPINACH FNR MODEL AS A GUIDE (KARPLUS, DANIELS, HERRIOTT, SCIENCE 1991, 251 60-66). RESIDUES 1 - 8 AND 106 - 112 ARE POORLY DEFINED IN THE ELECTRON DENSITY MAP AND THEY HAVE BEEN TENTATIVELY MODELED. WATER MOLECULES HAVE BEEN NUMBERED ACCORDING THE INCREASING VALUES OF THEIR TEMPERATURE FACTORS STARTING WITH 401. WATER SITES CLOSER THAN 2.5 ANGSTROMS TO PROTEIN ATOMS OR OTHER WATER SITES REFLECTS, MOST PROBABLY, DISORDER.
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Displacement parameters | Biso mean: 14.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å / Luzzati d res low obs: 15 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.82 Å
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Xplor file |
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