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- PDB-2hlf: Structure of the Escherichis coli ClC chloride channel Y445E muta... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hlf | ||||||
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Title | Structure of the Escherichis coli ClC chloride channel Y445E mutant and Fab complex | ||||||
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Function / homology | ![]() chloride:proton antiporter activity / cellular stress response to acidic pH / voltage-gated chloride channel activity / immunoglobulin complex, circulating / immunoglobulin receptor binding / chloride transmembrane transport / proton transmembrane transport / ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Accardi, A. / Lobet, S. / Williams, C. / Miller, C. / Dutzler, R. | ||||||
![]() | ![]() Title: Synergism Between Halide Binding and Proton Transport in a CLC-type Exchanger Authors: Accardi, A. / Lobet, S. / Williams, C. / Miller, C. / Dutzler, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 336.4 KB | Display | ![]() |
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PDB format | ![]() | 271.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2ht2C ![]() 2ht3C ![]() 2ht4C ![]() 2htkC ![]() 2htlC ![]() 1otsS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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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: 2 / Auth seq-ID: 18 - 458 / Label seq-ID: 2 - 442
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Components
#1: Protein | Mass: 47323.969 Da / Num. of mol.: 2 / Mutation: Y445E Source method: isolated from a genetically manipulated source Details: Each subunit of the mutant has a single Br- ion bound in the selectivity filter Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() #2: Antibody | ![]() Mass: 23693.918 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 | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.87 Å3/Da / Density % sol: 68.26 % |
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 9.5 Details: 34% peg 200/300 1:2, 50mM glycin, 150mM NaBr, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 24, 2005 |
Radiation | Monochromator: LN2 cooled fixed-exit Si(111) monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3.3→50 Å / Num. all: 44455 / Num. obs: 42596 / % possible obs: 95.8 % / Observed criterion σ(I): 1 / Biso Wilson estimate: 109 Å2 |
Reflection shell | Resolution: 3.3→3.42 Å / % possible all: 81.7 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1OTS Resolution: 3.3→40 Å / Cor.coef. Fo:Fc: 0.921 / Cor.coef. Fo:Fc free: 0.902 / Isotropic thermal model: restrained / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.543 / ESU R Free: 0.597 / Stereochemistry target values: Engh & Huber
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 128.436 Å2
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Refinement step | Cycle: LAST / Resolution: 3.3→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.3→3.385 Å / Total num. of bins used: 20
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