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Yorodumi- PDB-1go2: Structure of Ferredoxin-NADP+ Reductase with Lys 72 replaced by G... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1go2 | ||||||
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Title | Structure of Ferredoxin-NADP+ Reductase with Lys 72 replaced by Glu (K72E) | ||||||
Components | FERREDOXIN--NADP+ REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / FLAVOPROTEIN / FNR / ELECTRON TRANSPORT | ||||||
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 / NADP binding / flavin adenine dinucleotide binding Similarity search - Function | ||||||
Biological species | NOSTOC SP. (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Hermoso, J.A. / Mayoral, T. / Medina, M. / Sanz-Aparicio, J. / Gomez-Moreno, C. | ||||||
Citation | Journal: Proteins: Struct.,Funct., Genet. / Year: 2005 Title: Structural Analysis of Interactions for Complex Formation between Ferredoxin-Nadp+ Reductase and its Protein Partners Authors: Mayoral, T. / Martinez-Julvez, M. / Perez-Dorado, I. / Sanz-Aparicio, J. / Gomez-Moreno, C. / Medina, M. / Hermoso, J.A. #1: Journal: J.Mol.Biol. / Year: 1996 Title: X-Ray Structure of the Ferredoxin:Nadp+ Reductase from the Cyanobacterium Anabanena Pcc 7119 at 1.8A Resolution, and Crystallographic Studies of Nadp Binding at 2.25A Resolution Authors: Serre, L. / Vellieux, F.M.D. / Medina, M. / Gomez-Moreno, C. / Fontecilla, J.C. / Frey, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1go2.cif.gz | 82.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1go2.ent.gz | 59.8 KB | Display | PDB format |
PDBx/mmJSON format | 1go2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1go2_validation.pdf.gz | 474.5 KB | Display | wwPDB validaton report |
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Full document | 1go2_full_validation.pdf.gz | 476.8 KB | Display | |
Data in XML | 1go2_validation.xml.gz | 8 KB | Display | |
Data in CIF | 1go2_validation.cif.gz | 13.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/go/1go2 ftp://data.pdbj.org/pub/pdb/validation_reports/go/1go2 | HTTPS FTP |
-Related structure data
Related structure data | 1e62C 1e63C 1e64C 1qgyC 1queS C: citing same article (ref.) 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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Unit cell |
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-Components
#1: Protein | Mass: 34172.805 Da / Num. of mol.: 1 / Fragment: RESIDUES 137-440 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) NOSTOC SP. (bacteria) / Strain: PCC 7119 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P21890, ferredoxin-NADP+ reductase |
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#2: Chemical | ChemComp-FAD / |
#3: Chemical | ChemComp-SO4 / |
#4: Water | ChemComp-HOH / |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.3 Å3/Da / Density % sol: 63 % |
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Crystal grow | pH: 5 / Details: pH 5.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: D2AM / Wavelength: 1.01 |
Detector | Detector: CCD / Date: May 15, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.01 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→22.19 Å / Num. obs: 43287 / % possible obs: 98 % / Observed criterion σ(I): 3 / Redundancy: 4 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 1.71→1.79 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 2.2 / % possible all: 98 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1QUE Resolution: 1.7→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: 11.65 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.78 Å / Total num. of bins used: 8
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