[English] 日本語
![](img/lk-miru.gif)
- PDB-1ots: Structure of the Escherichia coli ClC Chloride channel and Fab Complex -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1ots | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of the Escherichia coli ClC Chloride channel and Fab Complex | ||||||
![]() |
| ||||||
![]() | MEMBRANE PROTEIN / ClC Chloride channel / Fab complex | ||||||
Function / homology | ![]() chloride:proton antiporter activity / cellular stress response to acidic pH / voltage-gated chloride channel activity / immunoglobulin complex / immunoglobulin mediated immune response / chloride transmembrane transport / proton transmembrane transport / B cell differentiation / antigen binding / blood microparticle ...chloride:proton antiporter activity / cellular stress response to acidic pH / voltage-gated chloride channel activity / immunoglobulin complex / immunoglobulin mediated immune response / chloride transmembrane transport / proton transmembrane transport / B cell differentiation / antigen binding / blood microparticle / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dutzler, R. / Campbell, E.B. / MacKinnon, R. | ||||||
![]() | ![]() Title: Gating the Selectivity Filter in ClC Chloride Channels Authors: Dutzler, R. / Campbell, E.B. / MacKinnon, R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 342.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 277.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 486.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 570 KB | Display | |
Data in XML | ![]() | 73.5 KB | Display | |
Data in CIF | ![]() | 100.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ottC ![]() 1otuC ![]() 1k4cS C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | the biological assembly for the ClC channel is a dimer formed by chain A and B / C and D are the heavy and light chain of a Fab fragment. E and F are the heavy and light chain of a Fab fragment. |
-
Components
#1: Protein | Mass: 49658.695 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Antibody | Mass: 23823.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Antibody | Mass: 23088.443 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #4: Chemical | ChemComp-CL / #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.55 Å3/Da / Density % sol: 65.05 % | ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 9.5 Details: PEG 300, sodium chloride, glycine, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K | ||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 25, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→35 Å / Num. all: 91182 / Num. obs: 88082 / % possible obs: 96.6 % / Observed criterion σ(I): 1 / Biso Wilson estimate: 70 Å2 / Rmerge(I) obs: 0.048 |
Reflection shell | Resolution: 2.5→2.59 Å / Rmerge(I) obs: 0.569 / Mean I/σ(I) obs: 2.3 / Num. unique all: 8532 / % possible all: 94.1 |
Reflection | *PLUS Lowest resolution: 35 Å |
Reflection shell | *PLUS % possible obs: 94.1 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: FAB fragment 1K4C Resolution: 2.51→24.58 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 2476756.08 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 40.5869 Å2 / ksol: 0.318637 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 69.2 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error free: 0.58 Å / Luzzati sigma a free: 0.63 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.51→24.58 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.5→2.66 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|