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Yorodumi- PDB-3fb6: KcsA Potassium channel in the partially open state with 16 A open... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 3fb6 | ||||||
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| Title | KcsA Potassium channel in the partially open state with 16 A opening at T112 | ||||||
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 informationaction potential / voltage-gated potassium channel activity / voltage-gated potassium channel complex / B cell differentiation / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
| Biological species | Streptomyces lividans (bacteria)![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Cuello, L.G. / Jogini, V. / Cortes, D.M. / Perozo, E. | ||||||
Citation | Journal: TO BE PUBLISHEDTitle: KcsA Potassium channel in the partially open state with 16 A opening at T112 Authors: Cuello, L.G. / Jogini, V. / Cortes, D.M. / Perozo, E. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 3fb6.cif.gz | 110.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3fb6.ent.gz | 85 KB | Display | PDB format |
| PDBx/mmJSON format | 3fb6.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3fb6_validation.pdf.gz | 435.3 KB | Display | wwPDB validaton report |
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| Full document | 3fb6_full_validation.pdf.gz | 445.3 KB | Display | |
| Data in XML | 3fb6_validation.xml.gz | 20.7 KB | Display | |
| Data in CIF | 3fb6_validation.cif.gz | 27.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fb/3fb6 ftp://data.pdbj.org/pub/pdb/validation_reports/fb/3fb6 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1k4cS 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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| 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) ![]() | ||
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| #2: Antibody | Mass: 23435.738 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||
| #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: ![]() | ||
| #4: Chemical | ChemComp-K / Has protein modification | Y | |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.89 Å3/Da / Density % sol: 68.35 % |
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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, pH 5-6, 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: Oct 13, 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→40 Å / Num. all: 17949 / Num. obs: 17088 / % possible obs: 95.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB entry 1K4C Resolution: 3→40 Å / σ(F): 2
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| Refinement step | Cycle: LAST / Resolution: 3→40 Å
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| Refine LS restraints |
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Streptomyces lividans (bacteria)
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