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Yorodumi- PDB-2ndj: Structural Basis for KCNE3 and Estrogen Modulation of the KCNQ1 C... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ndj | ||||||
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Title | Structural Basis for KCNE3 and Estrogen Modulation of the KCNQ1 Channel | ||||||
Components | Potassium voltage-gated channel subfamily E member 3 | ||||||
Keywords | MEMBRANE PROTEIN / Estrogen / Ion channel | ||||||
Function / homology | Function and homology information negative regulation of membrane repolarization during ventricular cardiac muscle cell action potential / negative regulation of potassium ion export across plasma membrane / basolateral part of cell / negative regulation of voltage-gated potassium channel activity / Phase 3 - rapid repolarisation / membrane repolarization during action potential / Phase 2 - plateau phase / intracellular chloride ion homeostasis / negative regulation of delayed rectifier potassium channel activity / potassium ion export across plasma membrane ...negative regulation of membrane repolarization during ventricular cardiac muscle cell action potential / negative regulation of potassium ion export across plasma membrane / basolateral part of cell / negative regulation of voltage-gated potassium channel activity / Phase 3 - rapid repolarisation / membrane repolarization during action potential / Phase 2 - plateau phase / intracellular chloride ion homeostasis / negative regulation of delayed rectifier potassium channel activity / potassium ion export across plasma membrane / voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization / ventricular cardiac muscle cell action potential / regulation of ventricular cardiac muscle cell membrane repolarization / delayed rectifier potassium channel activity / monoatomic ion channel complex / sodium ion transport / neuronal cell body membrane / regulation of heart rate by cardiac conduction / potassium channel regulator activity / perikaryon / vesicle / transmembrane transporter binding / membrane raft / dendrite / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing, molecular dynamics | ||||||
Model details | closest to the average, model3 | ||||||
Authors | Sanders, C.R. / Van Horn, W.D. / Kroncke, B.M. / Sisco, N.J. / Meiler, J. / Vanoye, C.G. / Song, Y. / Nannemann, D.P. / Welch, R.C. / Kang, C. ...Sanders, C.R. / Van Horn, W.D. / Kroncke, B.M. / Sisco, N.J. / Meiler, J. / Vanoye, C.G. / Song, Y. / Nannemann, D.P. / Welch, R.C. / Kang, C. / Smith, J. / George, A.L. | ||||||
Citation | Journal: Sci Adv / Year: 2016 Title: Structural basis for KCNE3 modulation of potassium recycling in epithelia. Authors: Kroncke, B.M. / Van Horn, W.D. / Smith, J. / Kang, C. / Welch, R.C. / Song, Y. / Nannemann, D.P. / Taylor, K.C. / Sisco, N.J. / George, A.L. / Meiler, J. / Vanoye, C.G. / Sanders, C.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ndj.cif.gz | 334.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ndj.ent.gz | 276.9 KB | Display | PDB format |
PDBx/mmJSON format | 2ndj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ndj_validation.pdf.gz | 543.5 KB | Display | wwPDB validaton report |
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Full document | 2ndj_full_validation.pdf.gz | 748.2 KB | Display | |
Data in XML | 2ndj_validation.xml.gz | 54.3 KB | Display | |
Data in CIF | 2ndj_validation.cif.gz | 55.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nd/2ndj ftp://data.pdbj.org/pub/pdb/validation_reports/nd/2ndj | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12799.581 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCNE3, MiRP2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / Variant (production host): (DE3) RP Codon Plus / References: UniProt: Q9Y6H6 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.8 mM [U-100% 13C; U-100% 15N; U-80% 2H] protein, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.8 mM / Component: entity-1 / Isotopic labeling: [U-100% 13C; U-100% 15N; U-80% 2H] |
Sample conditions | pH: 6.5 / Temperature: 313 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing, molecular dynamics Software ordinal: 1 | |||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 189 / NOE long range total count: 0 / NOE medium range total count: 79 / NOE sequential total count: 110 / Protein phi angle constraints total count: 98 / Protein psi angle constraints total count: 98 | |||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | |||||||||||||||||||||||||||||||||
NMR ensemble | Average torsion angle constraint violation: 0 ° Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 9764 / Conformers submitted total number: 10 / Maximum torsion angle constraint violation: 5.544 ° / Torsion angle constraint violation method: Xplor-NIH, Amber |