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Yorodumi- PDB-3k0g: Crystal Structure of CNG mimicking NaK mutant, NaK-ETPP, Na+ complex -
+Open data
-Basic information
Entry | Database: PDB / ID: 3k0g | ||||||
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Title | Crystal Structure of CNG mimicking NaK mutant, NaK-ETPP, Na+ complex | ||||||
Components | Potassium channel protein NaK | ||||||
Keywords | TRANSPORT PROTEIN / NaK-ETPP / ETPP / NaK / CNG mimicking / CNG channel selectivity filter / NaK-mutant / Ionic channel | ||||||
Function / homology | Function and homology information stabilization of membrane potential / potassium ion leak channel activity / outward rectifier potassium channel activity / identical protein binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | Bacillus cereus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å | ||||||
Authors | Jiang, Y. / Derebe, M.G. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2011 Title: Structural studies of ion permeation and Ca2+ blockage of a bacterial channel mimicking the cyclic nucleotide-gated channel pore. Authors: Derebe, M.G. / Zeng, W. / Li, Y. / Alam, A. / Jiang, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3k0g.cif.gz | 51 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3k0g.ent.gz | 37 KB | Display | PDB format |
PDBx/mmJSON format | 3k0g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3k0g_validation.pdf.gz | 458.5 KB | Display | wwPDB validaton report |
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Full document | 3k0g_full_validation.pdf.gz | 463.4 KB | Display | |
Data in XML | 3k0g_validation.xml.gz | 11.1 KB | Display | |
Data in CIF | 3k0g_validation.cif.gz | 13.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k0/3k0g ftp://data.pdbj.org/pub/pdb/validation_reports/k0/3k0g | HTTPS FTP |
-Related structure data
-Links
-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: Protein | Mass: 10626.555 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus cereus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: Q81HW2 #2: Chemical | ChemComp-MPD / ( #3: Chemical | ChemComp-NA / #4: Water | ChemComp-HOH / | Sequence details | AT THE REGION, FOUR RESIDUES ETPP WERE USED TO REPLACE THE FIVE RESIDUES DGNFS IN THE UNP SEQUENCE REFERENCE. | |
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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: 2.4 Å3/Da / Density % sol: 48.84 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion Details: MPD, NaCl, pH 6.5-8.5, vapor diffusion, temperature 293K PH range: 6.5-8.5 |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID |
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Detector | Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Highest resolution: 1.95 Å / Num. obs: 14710 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Highest resolution: 1.95 Å / Occupancy max: 1 / Occupancy min: 1 / σ(F): 0
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Solvent computation | Bsol: 136.199 Å2 | ||||||||||||||||
Displacement parameters | Biso max: 95.41 Å2 / Biso mean: 42.642 Å2 / Biso min: 13.76 Å2
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Refinement step | Cycle: LAST / Highest resolution: 1.95 Å
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Refine LS restraints |
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Xplor file |
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