[English] 日本語
![](img/lk-miru.gif)
- PDB-2fed: Structure of the E203Q mutant of the Cl-/H+ exchanger CLC-ec1 fro... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2fed | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of the E203Q mutant of the Cl-/H+ exchanger CLC-ec1 from E.Coli | ||||||
![]() |
| ||||||
![]() | PROTON TRANSPORT / MEMBRANE PROTEIN / CLC-ec1 / CLCA_ECOLI / Chloride/Proton exchange transporter | ||||||
Function / homology | ![]() chloride:proton antiporter activity / cellular stress response to acidic pH / voltage-gated chloride channel activity / chloride transmembrane transport / proton transmembrane transport / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Accardi, A. / Walden, M.P. / Nguitragool, W. / Jayaram, H. / Williams, C. / Miller, C. | ||||||
![]() | ![]() Title: Separate ion pathways in a Cl-/H+ exchanger Authors: Accardi, A. / Walden, M.P. / Nguitragool, W. / Jayaram, H. / Williams, C. / Miller, C. #1: ![]() Title: Gating the selectivity filter in ClC chloride channels Authors: Dutzler, R. / Cambell, E.B. / Mackinnon, R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 325.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 265.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 477 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 511 KB | Display | |
Data in XML | ![]() | 58.9 KB | Display | |
Data in CIF | ![]() | 80.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2fecC ![]() 2feeC ![]() 1otsS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||||
Unit cell |
| ||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ARG / Beg label comp-ID: ARG / End auth comp-ID: ALA / End label comp-ID: ALA / Refine code: 3 / Auth seq-ID: 18 - 458 / Label seq-ID: 18 - 458
|
-
Components
#1: Protein | Mass: 49657.711 Da / Num. of mol.: 2 / Mutation: E203Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Antibody | Mass: 23823.031 Da / Num. of mol.: 2 / Fragment: Heavy Chain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Antibody | Mass: 23088.443 Da / Num. of mol.: 2 / Fragment: Light Chain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.73 Å3/Da / Density % sol: 67.05 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 250 mM NaCl, PEG 400 37%, 0.05 M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9198 Å / Relative weight: 1 |
Reflection | Resolution: 3.317→49.81 Å / Num. obs: 36343 / % possible obs: 88.3 % / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.096 / Net I/σ(I): 13.4 |
Reflection shell | Resolution: 3.317→3.42 Å / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 2.1 / Rsym value: 0.47 / % possible all: 85.5 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 1OTS Resolution: 3.317→49.81 Å / Cor.coef. Fo:Fc: 0.889 / Cor.coef. Fo:Fc free: 0.87 / SU B: 28.98 / SU ML: 0.475 / Cross valid method: THROUGHOUT / σ(F): 3 / ESU R Free: 0.583 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 94.826 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.317→49.81 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints NCS | Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 3.317→3.403 Å / Total num. of bins used: 20
|