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- PDB-3kvt: TETRAMERIZATION DOMAIN FROM AKV3.1 (SHAW-SUBFAMILY) VOLTAGE-GATED... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3kvt | ||||||
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Title | TETRAMERIZATION DOMAIN FROM AKV3.1 (SHAW-SUBFAMILY) VOLTAGE-GATED POTASSIUM CHANNEL | ||||||
![]() | POTASSIUM CHANNEL PROTEIN SHAW | ||||||
![]() | POTASSIUM CHANNEL / TETRAMERIZATION DOMAIN / MOLECULAR RECOGNITION / ZINC-BINDING | ||||||
Function / homology | ![]() regulation of monoatomic ion transmembrane transport / voltage-gated potassium channel activity / voltage-gated potassium channel complex / protein homooligomerization / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bixby, K.A. / Nanao, M.H. / Shen, N.V. / Kreusch, A. / Bellamy, H. / Pfaffinger, P.J. / Choe, S. | ||||||
![]() | ![]() Title: Zn2+-binding and molecular determinants of tetramerization in voltage-gated K+ channels. Authors: Bixby, K.A. / Nanao, M.H. / Shen, N.V. / Kreusch, A. / Bellamy, H. / Pfaffinger, P.J. / Choe, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 36.6 KB | Display | ![]() |
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PDB format | ![]() | 23.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 359.9 KB | Display | ![]() |
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Full document | ![]() | 359.9 KB | Display | |
Data in XML | ![]() | 3.3 KB | Display | |
Data in CIF | ![]() | 4.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 13389.151 Da / Num. of mol.: 1 / Fragment: TETRAMERIZATION (T1) DOMAIN / Mutation: A42G, L43M, A44L Source method: isolated from a genetically manipulated source Details: ONE ZN2+ PER MONOMER TETRAHEDRALLY COORDINATED AT MONOMER-MONOMER INTERFACE Source: (gene. exp.) ![]() ![]() Tissue: NERVE / Cell line: BL21 PLYS S / Cellular location: MEMBRANE / Plasmid: PET16B / Cell line (production host): BL21 PLYS S / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 51 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 1, 1997 / Details: PLATINUM COATED MIRRORS |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 2→25 Å / Num. obs: 11135 / % possible obs: 99.8 % / Redundancy: 11.3 % / Biso Wilson estimate: 18.7 Å2 / Rsym value: 0.057 |
Reflection shell | Resolution: 2→2.07 Å / Rsym value: 0.401 / % possible all: 99.5 |
Reflection | *PLUS Num. measured all: 126110 / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS % possible obs: 99.5 % / Rmerge(I) obs: 0.401 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1AP61 Resolution: 2→25 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 28.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.07 Å / Rfactor Rfree error: 0.04 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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