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Yorodumi- PDB-1kn7: Solution structure of the tandem inactivation domain (residues 1-... -
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-Basic information
Entry | Database: PDB / ID: 1kn7 | ||||||
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Title | Solution structure of the tandem inactivation domain (residues 1-75) of potassium channel RCK4 (Kv1.4) | ||||||
Components | VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV1.4 | ||||||
Keywords | MEMBRANE PROTEIN / voltage-gated potassium channel / inactivation domain / Kv1.4 / RCK4 | ||||||
Function / homology | Function and homology information regulation of presynaptic membrane potential / Voltage gated Potassium channels / axon initial segment / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / delayed rectifier potassium channel activity / action potential / potassium ion binding / voltage-gated potassium channel activity / potassium channel activity / asymmetric synapse ...regulation of presynaptic membrane potential / Voltage gated Potassium channels / axon initial segment / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / delayed rectifier potassium channel activity / action potential / potassium ion binding / voltage-gated potassium channel activity / potassium channel activity / asymmetric synapse / voltage-gated potassium channel complex / potassium ion transmembrane transport / monoatomic ion channel activity / dendritic shaft / protein homooligomerization / potassium ion transport / monoatomic ion transmembrane transport / presynaptic membrane / postsynaptic membrane / dendritic spine / axon / glutamatergic synapse / cell surface / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Authors | Wissmann, R. / Bildl, W. / Oliver, D. / Beyermann, M. / Kalbitzer, H.R. / Bentrop, D. / Fakler, B. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003 Title: Solution Structure and Function of the "Tandem Inactivation Domain" of the Neuronal A-type Potassium Channel Kv1.4 Authors: Wissmann, R. / Bildl, W. / Oliver, D. / Beyermann, M. / Kalbitzer, H.R. / Bentrop, D. / Fakler, B. | ||||||
History |
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Remark 999 | SEQUENCE The protein construct used in this study contains three additional residues at the N- ...SEQUENCE The protein construct used in this study contains three additional residues at the N-terminus from a thrombin cleavage site (Gly-Ser-Thr). |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kn7.cif.gz | 497.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kn7.ent.gz | 421.4 KB | Display | PDB format |
PDBx/mmJSON format | 1kn7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1kn7_validation.pdf.gz | 346.4 KB | Display | wwPDB validaton report |
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Full document | 1kn7_full_validation.pdf.gz | 503.7 KB | Display | |
Data in XML | 1kn7_validation.xml.gz | 28.5 KB | Display | |
Data in CIF | 1kn7_validation.cif.gz | 45.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kn/1kn7 ftp://data.pdbj.org/pub/pdb/validation_reports/kn/1kn7 | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7858.493 Da / Num. of mol.: 1 Fragment: N-terminal tandem inactivation domain (residues 1-75) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: KCNA4 / Plasmid: pET41a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P15385 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 50 mM / pH: 4.4 / Pressure: ambient / Temperature: 283 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 / Details: SEE THE PRIMARY CITATION FOR STRUCTURAL STATISTICS | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,target function Conformers calculated total number: 300 / Conformers submitted total number: 25 |