+
Open data
-
Basic information
Entry | Database: PDB / ID: 2a79 | ||||||
---|---|---|---|---|---|---|---|
Title | Mammalian Shaker Kv1.2 potassium channel- beta subunit complex | ||||||
![]() |
| ||||||
![]() | MEMBRANE PROTEIN / potassium channel / voltage sensor / voltage dependent / ion channel / Shaker / eukaryotic / Kv1.2 | ||||||
Function / homology | ![]() optic nerve structural organization / pinceau fiber / methylglyoxal reductase (NADPH) (acetol producing) activity / Voltage gated Potassium channels / potassium channel complex / voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / : / paranodal junction / regulation of circadian sleep/wake cycle, non-REM sleep / potassium ion export across plasma membrane ...optic nerve structural organization / pinceau fiber / methylglyoxal reductase (NADPH) (acetol producing) activity / Voltage gated Potassium channels / potassium channel complex / voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / : / paranodal junction / regulation of circadian sleep/wake cycle, non-REM sleep / potassium ion export across plasma membrane / regulation of protein localization to cell surface / corpus callosum development / delayed rectifier potassium channel activity / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / : / axon initial segment / juxtaparanode region of axon / Oxidoreductases; Acting on the CH-OH group of donors; With NAD+ or NADP+ as acceptor / outward rectifier potassium channel activity / myoblast differentiation / regulation of potassium ion transmembrane transport / Neutrophil degranulation / optic nerve development / neuronal cell body membrane / neuromuscular process / regulation of dopamine secretion / lamellipodium membrane / action potential / kinesin binding / voltage-gated potassium channel activity / potassium channel regulator activity / hematopoietic progenitor cell differentiation / neuronal action potential / axon terminus / voltage-gated potassium channel complex / sensory perception of pain / potassium ion transmembrane transport / calyx of Held / postsynaptic density membrane / protein homooligomerization / cerebral cortex development / cytoplasmic side of plasma membrane / lamellipodium / presynaptic membrane / perikaryon / transmembrane transporter binding / postsynaptic membrane / cytoskeleton / neuron projection / postsynaptic density / endosome / axon / dendrite / endoplasmic reticulum membrane / protein-containing complex binding / glutamatergic synapse / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Long, S.B. / Campbell, E.B. / MacKinnon, R. | ||||||
![]() | ![]() Title: Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Authors: Long, S.B. / Campbell, E.B. / Mackinnon, R. #1: ![]() Title: Voltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling Authors: Long, S.B. / Campbell, E.B. / MacKinnon, R. | ||||||
History |
| ||||||
Remark 999 | SEQUENCE SEE REMARK 3, OTHER REFINEMENT REMARKS, FOR DETAILS REGARDING POLY-UNKNOWN CHAINS C AND D ...SEQUENCE SEE REMARK 3, OTHER REFINEMENT REMARKS, FOR DETAILS REGARDING POLY-UNKNOWN CHAINS C AND D AND THEIR RELATIONSHIP TO CHAIN B. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 147.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 108.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 1exbS S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| |||||||||||||||||||||
Unit cell |
| |||||||||||||||||||||
Components on special symmetry positions |
| |||||||||||||||||||||
Details | The biological unit is a tetramer formed by applying the I4 crystallographic symmetry to the coordinates that are deposited. |
-
Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 37353.086 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Protein | Mass: 56749.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Poly-unknown ... , 2 types, 2 molecules CD
#3: Protein | Mass: 4443.468 Da / Num. of mol.: 1 / Fragment: T1-S1 linker and S1 helix of the Kv1.2 channel Source method: isolated from a genetically manipulated source Details: Chain C consists of a polyglycine model for the T1-S1 linker and a polyalanine model for the S1 helix of Kv1.2. Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#4: Protein/peptide | Mass: 1805.216 Da / Num. of mol.: 1 / Fragment: S3 helix of the Kv1.2 channel Source method: isolated from a genetically manipulated source Details: Chain D consists of a polyalanine model for the S3 helix of Kv1.2. Source: (gene. exp.) ![]() ![]() ![]() |
-Non-polymers , 3 types, 90 molecules 




#5: Chemical | ChemComp-NAP / | ||
---|---|---|---|
#6: Chemical | ChemComp-K / #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 4.47 Å3/Da / Density % sol: 68 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: peg 400, potassium chloride, tris buffer, EDTA, DTT, TCEP, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 3, 2005 / Details: NSLS X25 |
Radiation | Monochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→30 Å / Num. all: 36056 / Num. obs: 36056 / % possible obs: 99 % / Observed criterion σ(I): -3 / Redundancy: 2.92 % / Biso Wilson estimate: 60.4 Å2 / Rsym value: 0.072 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 2.9 % / Mean I/σ(I) obs: 2.1 / Num. unique all: 3636 / Rsym value: 0.477 / % possible all: 99.9 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1EXB Resolution: 2.9→29.48 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 4165737.46 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: Some of the missing residues listed in remark 465 are actually the residues that comprise chains C and D. The authors state it is unclear how to align the residues of chains C and D to the ...Details: Some of the missing residues listed in remark 465 are actually the residues that comprise chains C and D. The authors state it is unclear how to align the residues of chains C and D to the sequence of chain B, so each stretch of density assigned chain IDs C and D is labelled as UNK for unknown residue and was modelled in refinement as alanine or glycine.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 50.2425 Å2 / ksol: 0.295433 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 89.1 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→29.48 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.9→3 Å / Rfactor Rfree error: 0.031 / Total num. of bins used: 10
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
|