+Open data
-Basic information
Entry | Database: PDB / ID: 2k44 | ||||||
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Title | Solution structure of a K+-channel voltage-sensor paddle domain | ||||||
Components | K+-channel voltage-sensor paddle domain of Calcium-activated potassium channel subunit alpha-1 | ||||||
Keywords | MEMBRANE PROTEIN / potassium channel / voltage-sensor / membrane / micelle / solution structure | ||||||
Function / homology | Function and homology information Acetylcholine inhibits contraction of outer hair cells / micturition / Ca2+ activated K+ channels / large conductance calcium-activated potassium channel activity / response to carbon monoxide / calcium-activated potassium channel activity / negative regulation of cell volume / intracellular potassium ion homeostasis / smooth muscle contraction involved in micturition / Sensory processing of sound by inner hair cells of the cochlea ...Acetylcholine inhibits contraction of outer hair cells / micturition / Ca2+ activated K+ channels / large conductance calcium-activated potassium channel activity / response to carbon monoxide / calcium-activated potassium channel activity / negative regulation of cell volume / intracellular potassium ion homeostasis / smooth muscle contraction involved in micturition / Sensory processing of sound by inner hair cells of the cochlea / response to osmotic stress / voltage-gated potassium channel activity / cGMP effects / voltage-gated potassium channel complex / potassium ion transmembrane transport / regulation of membrane potential / caveola / potassium ion transport / response to calcium ion / vasodilation / actin binding / postsynaptic membrane / response to hypoxia / positive regulation of apoptotic process / apical plasma membrane / membrane / identical protein binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | NMR solution structure of a putative S3b-S4 domain of HsapBK(233-260) in DPC micelles | ||||||
Authors | Unnerstale, S. / Lind, J. / Papadopoulos, E. / Maler, L. | ||||||
Citation | Journal: Biochemistry / Year: 2009 Title: Solution structure of the HsapBK K+-channel voltage-sensor paddle sequence Authors: Unnerstale, S. / Lind, J. / Papadopoulos, E. / Maler, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k44.cif.gz | 332.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2k44.ent.gz | 283.9 KB | Display | PDB format |
PDBx/mmJSON format | 2k44.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k4/2k44 ftp://data.pdbj.org/pub/pdb/validation_reports/k4/2k44 | HTTPS FTP |
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-Related structure data
Similar structure data |
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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/peptide | Mass: 3385.016 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic peptide / References: UniProt: Q12791 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: NMR solution structure of a putative S3b-S4 domain of HsapBK(233-260) in DPC micelles | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 100mM [U-2H] 98% DPC, 50mM potassium chloride, 1mM HsapBK(233-260), 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.05 / pH: 5.5 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 / Details: CYANA 2.0 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 30 / Representative conformer: 1 |