+Open data
-Basic information
Entry | Database: PDB / ID: 3fb7 | ||||||
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Title | Open KcsA potassium channel in the presence of Rb+ ion | ||||||
Components |
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Keywords | membrane protein/metal transport / kcsa / open / inactivation / potassium channel / Cell membrane / Ion transport / Ionic channel / Membrane / Transmembrane / Transport / Voltage-gated channel / membrane protein-metal transport COMPLEX | ||||||
Function / homology | Function and homology information delayed rectifier potassium channel activity / voltage-gated potassium channel complex / identical protein binding Similarity search - Function | ||||||
Biological species | Streptomyces lividans (bacteria) Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å | ||||||
Authors | Cuello, L.G. / Jogini, V. / Cortes, D.M. / Pan, A.C. / Gagnon, D.H. / Cordero-Morales, J.F. / Chakrapani, S. / Roux, B. / Perozo, E. | ||||||
Citation | Journal: TO BE PUBLISHED Title: Open KcsA potassium channel in the presence of Rb+ ion Authors: Cuello, L.G. / Jogini, V. / Cortes, D.M. / Pan, A.C. / Gagnon, D.H. / Cordero-Morales, J.F. / Chakrapani, S. / Roux, B. / Perozo, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3fb7.cif.gz | 111.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3fb7.ent.gz | 85.8 KB | Display | PDB format |
PDBx/mmJSON format | 3fb7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3fb7_validation.pdf.gz | 437.2 KB | Display | wwPDB validaton report |
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Full document | 3fb7_full_validation.pdf.gz | 454.8 KB | Display | |
Data in XML | 3fb7_validation.xml.gz | 21.9 KB | Display | |
Data in CIF | 3fb7_validation.cif.gz | 29.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fb/3fb7 ftp://data.pdbj.org/pub/pdb/validation_reports/fb/3fb7 | HTTPS FTP |
-Related structure data
Related structure data | 1k4cS 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 on special symmetry positions |
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-Components
#1: Antibody | Mass: 23411.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) |
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#2: Antibody | Mass: 23435.738 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) |
#3: Protein | Mass: 10927.571 Da / Num. of mol.: 1 / Fragment: UNP residues 21-124 / Mutation: H25Q,L90C,R117Q,E120Q,R121Q,R122Q,H124Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces lividans (bacteria) / Gene: kcsA, skc1 / Production host: Escherichia coli (E. coli) / Strain (production host): XL10-Gold / References: UniProt: P0A334 |
#4: Chemical | ChemComp-RB / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.98 Å3/Da / Density % sol: 69.1 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: 20-25% PEG400, 50mM magnesium acetate, 50mM sodium acetate pH 5.0-6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K PH range: 5-6 |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 1 Å |
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Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 19, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→50 Å / Num. all: 13859 / Num. obs: 13294 / % possible obs: 95.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1K4C Resolution: 3.3→50 Å / σ(F): 2
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3.3→50 Å
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Refine LS restraints |
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