+Open data
-Basic information
Entry | Database: PDB / ID: 1s1g | ||||||
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Title | Crystal Structure of Kv4.3 T1 Domain | ||||||
Components | Potassium voltage-gated channel subfamily D member 3 | ||||||
Keywords | TRANSPORT PROTEIN / K+ channels / tetramerization domain / T1 domain | ||||||
Function / homology | Function and homology information ventricular cardiac muscle cell membrane repolarization / Kv4.3-KChIP1 channel complex / A-type (transient outward) potassium channel activity / Phase 1 - inactivation of fast Na+ channels / membrane repolarization during ventricular cardiac muscle cell action potential / membrane repolarization during cardiac muscle cell action potential / potassium ion export across plasma membrane / membrane repolarization / Voltage gated Potassium channels / postsynaptic specialization membrane ...ventricular cardiac muscle cell membrane repolarization / Kv4.3-KChIP1 channel complex / A-type (transient outward) potassium channel activity / Phase 1 - inactivation of fast Na+ channels / membrane repolarization during ventricular cardiac muscle cell action potential / membrane repolarization during cardiac muscle cell action potential / potassium ion export across plasma membrane / membrane repolarization / Voltage gated Potassium channels / postsynaptic specialization membrane / regulation of heart contraction / action potential / regulation of heart rate by cardiac conduction / voltage-gated potassium channel activity / voltage-gated potassium channel complex / GABA-ergic synapse / muscle contraction / potassium ion transmembrane transport / protein tetramerization / potassium ion transport / protein homooligomerization / sarcolemma / chemical synaptic transmission / postsynaptic membrane / transmembrane transporter binding / dendritic spine / neuronal cell body / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Scannevin, R.H. / Wang, K.W. / Jow, F. / Megules, J. / Kopsco, D.C. / Edris, W. / Carroll, K.C. / Lu, Q. / Xu, W.X. / Xu, Z.B. ...Scannevin, R.H. / Wang, K.W. / Jow, F. / Megules, J. / Kopsco, D.C. / Edris, W. / Carroll, K.C. / Lu, Q. / Xu, W.X. / Xu, Z.B. / Katz, A.H. / Olland, S. / Lin, L. / Taylor, M. / Stahl, M. / Malakian, K. / Somers, W. / Mosyak, L. / Bowlby, M.R. / Chanda, P. / Rhodes, K.J. | ||||||
Citation | Journal: Neuron / Year: 2004 Title: Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1. Authors: Scannevin, R.H. / Wang, K.W. / Jow, F. / Megules, J. / Kopsco, D.C. / Edris, W. / Carroll, K.C. / Xu, W.X. / Xu, Z.B. / Katz, A.H. / Olland, S. / Lin, L. / Taylor, M. / Stahl, M. / Malakian, ...Authors: Scannevin, R.H. / Wang, K.W. / Jow, F. / Megules, J. / Kopsco, D.C. / Edris, W. / Carroll, K.C. / Xu, W.X. / Xu, Z.B. / Katz, A.H. / Olland, S. / Lin, L. / Taylor, M. / Stahl, M. / Malakian, K. / Somers, W. / Mosyak, L. / Bowlby, M.R. / Chanda, P. / Rhodes, K.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1s1g.cif.gz | 60.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1s1g.ent.gz | 43.8 KB | Display | PDB format |
PDBx/mmJSON format | 1s1g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1s1g_validation.pdf.gz | 438.7 KB | Display | wwPDB validaton report |
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Full document | 1s1g_full_validation.pdf.gz | 444.9 KB | Display | |
Data in XML | 1s1g_validation.xml.gz | 11.2 KB | Display | |
Data in CIF | 1s1g_validation.cif.gz | 13.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s1/1s1g ftp://data.pdbj.org/pub/pdb/validation_reports/s1/1s1g | HTTPS FTP |
-Related structure data
Related structure data | 1s1eC 3kvtS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 15157.938 Da / Num. of mol.: 2 / Fragment: Kv4.3T1 (residue 29-143, SWS Q9Uk17) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCND3 / Plasmid: pET-21 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21-DE3 / References: UniProt: Q9UK17 #2: Chemical | #3: Water | ChemComp-HOH / | |
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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: 3.55 Å3/Da / Density % sol: 65.05 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 10.6 Details: Sodium Phosphate/Potassium Phosphate, Lisium Sulfate, CAPS, pH 10.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7.4 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 143 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1.1 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: May 6, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→20 Å / Num. all: 12111 / Num. obs: 12263 / % possible obs: 96.1 % / Observed criterion σ(F): 3 / Biso Wilson estimate: 44.8 Å2 / Rsym value: 0.071 |
Reflection shell | Resolution: 2.6→2.69 Å / Num. unique all: 995 / % possible all: 87 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB CODE 3kvt Resolution: 2.6→19.85 Å / Rfactor Rfree error: 0.011 / Data cutoff high absF: 160298.96 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 37.2124 Å2 / ksol: 0.367987 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 59.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→19.85 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.69 Å / Rfactor Rfree error: 0.052 / Total num. of bins used: 10
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 20 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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