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Yorodumi- PDB-1ott: Structure of the Escherichia coli ClC Chloride channel E148A muta... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ott | ||||||
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Title | Structure of the Escherichia coli ClC Chloride channel E148A mutant and Fab Complex | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / chloride channel / Fab complex / ion channel | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Dutzler, R. / Campbell, E.B. / MacKinnon, R. | ||||||
Citation | Journal: Science / Year: 2003 Title: Gating the Selectivity Filter in ClC Chloride Channels Authors: Dutzler, R. / Campbell, E.B. / MacKinnon, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ott.cif.gz | 332.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ott.ent.gz | 268.3 KB | Display | PDB format |
PDBx/mmJSON format | 1ott.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ot/1ott ftp://data.pdbj.org/pub/pdb/validation_reports/ot/1ott | HTTPS FTP |
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-Related structure data
Related structure data | 1otsSC 1otuC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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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: 49600.660 Da / Num. of mol.: 2 / Mutation: E148A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: ERIC OR B0155 / Plasmid: pet28b+ / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21DE3 / References: UniProt: P37019 #2: Antibody | Mass: 23823.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / Cell line: Hybridoma Cell line / References: UniProt: P01808*PLUS #3: Antibody | Mass: 23088.443 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / Cell line: Hybridoma Cell line / References: UniProt: P01837*PLUS #4: Chemical | ChemComp-CL / |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 67.48 % | ||||||||||||||||||||||||||||
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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
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Oct 15, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 3→35 Å / Num. all: 55723 / Num. obs: 52212 / % possible obs: 93.7 % / Observed criterion σ(I): 1 / Biso Wilson estimate: 71.2 Å2 / Rmerge(I) obs: 0.072 / Net I/σ(I): 14.8 |
Reflection shell | Resolution: 3→3.11 Å / Rmerge(I) obs: 0.492 / Mean I/σ(I) obs: 2.1 / % possible all: 76.2 |
Reflection | *PLUS Lowest resolution: 35 Å |
Reflection shell | *PLUS % possible obs: 76.2 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1OTS Resolution: 3→24.99 Å / Rfactor Rfree error: 0.007 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 20.8672 Å2 / ksol: 0.26162 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 79.8 Å2
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Refine analyze | Luzzati coordinate error free: 0.69 Å / Luzzati sigma a free: 0.94 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→24.99 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.19 Å / Rfactor Rfree error: 0.028 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 3 Å / Lowest resolution: 25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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