+Open data
-Basic information
Entry | Database: PDB / ID: 1ewy | ||||||
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Title | ANABAENA PCC7119 FERREDOXIN:FERREDOXIN-NADP+-REDUCTASE COMPLEX | ||||||
Components |
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Keywords | OXIDOREDUCTASE / ELECTRON TRANSFER COMPLEX / PHOTOSYNTHESIS / PROTEIN-PROTEIN INTERACTION / FERREDOXIN / REDUCTASE | ||||||
Function / homology | Function and homology information ferredoxin-NADP+ reductase / ferredoxin-NADP+ reductase activity / NADPH dehydrogenase activity / phycobilisome / plasma membrane-derived thylakoid membrane / electron transport chain / 2 iron, 2 sulfur cluster binding / NADP binding / flavin adenine dinucleotide binding / electron transfer activity / metal ion binding Similarity search - Function | ||||||
Biological species | Nostoc sp. PCC 7119 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.38 Å | ||||||
Authors | Morales, R. / Charon, M.H. / Frey, M. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2000 Title: Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule. Authors: Morales, R. / Kachalova, G. / Vellieux, F. / Charon, M.H. / Frey, M. #1: Journal: Embo J. / Year: 2000 Title: A Redox-Dependent Interaction between Two Electron-Transfer Partners Involved in Photosynthesis Authors: Morales, R. / Charon, M.H. / Kachalova, G. / Serre, L.S. / Medina, M. / Gomez-Moreno, C. / Frey, M. | ||||||
History |
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Remark 300 | The biological molecule consists of one ferredoxin-NADP reductase and one ferredoxin I. Biomolecule ...The biological molecule consists of one ferredoxin-NADP reductase and one ferredoxin I. Biomolecule 2 in REMARK 350 is meaningless. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ewy.cif.gz | 156.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ewy.ent.gz | 121.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ewy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ewy_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 1ewy_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 1ewy_validation.xml.gz | 34.8 KB | Display | |
Data in CIF | 1ewy_validation.cif.gz | 45.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ew/1ewy ftp://data.pdbj.org/pub/pdb/validation_reports/ew/1ewy | HTTPS FTP |
-Related structure data
Related structure data | 1queS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 34042.660 Da / Num. of mol.: 2 / Fragment: 138-440 / Source method: isolated from a natural source / Source: (natural) Nostoc sp. PCC 7119 (bacteria) / References: UniProt: P21890, ferredoxin-NADP+ reductase #2: Protein | | Mass: 10705.624 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Nostoc sp. PCC 7119 (bacteria) / References: UniProt: P0A3C8 #3: Chemical | #4: Chemical | ChemComp-FES / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.73 Å3/Da / Density % sol: 28.9 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 20-24% PEG 6000,10 mM MES pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 8 | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID2 / Wavelength: 0.98 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 6, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→30 Å / Num. all: 175226 / Num. obs: 25838 / % possible obs: 97.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.3 % / Biso Wilson estimate: 35 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 7.9 |
Reflection shell | Resolution: 2.28→2.5 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.077 / Mean I/σ(I) obs: 4.2 / Num. unique all: 2586 / % possible all: 87.7 |
Reflection | *PLUS Num. measured all: 175226 / Rmerge(I) obs: 0.046 |
Reflection shell | *PLUS % possible obs: 87.7 % / Rmerge(I) obs: 0.077 / Mean I/σ(I) obs: 7.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1QUE FOR FERREDOXIN-NADP+REDUCTASE Resolution: 2.38→15 Å / Num. parameters: 22871 / Num. restraintsaints: 23488 / Cross valid method: FREE R / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH AND HUBER Details: The Twin option in SHELX97 was used, with the TWIN 0 1 0 1 0 0 0 0 -1 2 command.
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Refine analyze | Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 5503 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.38→15 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 15 Å / Rfactor all: 0.232 / Rfactor obs: 0.219 / Rfactor Rfree: 0.292 / Rfactor Rwork: 0.219 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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