+Open data
-Basic information
Entry | Database: PDB / ID: 2atk | ||||||
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Title | Structure of a mutant KcsA K+ channel | ||||||
Components |
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Keywords | IMMUNE SYSTEM/ION TRANSPORT / K+ channel / mutant KcsA / protein-antibody Fab complex / IMMUNE SYSTEM-ION TRANSPORT COMPLEX | ||||||
Function / homology | Function and homology information delayed rectifier potassium channel activity / voltage-gated potassium channel complex / identical protein binding Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Streptomyces lividans (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Cordero-Morales, J.F. / Cuello, L.G. / Zhao, Y. / Jogini, V. / Chakrapani, S. / Roux, B. / Perozo, E. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2006 Title: Molecular determinants of gating at the potassium-channel selectivity filter. Authors: Cordero-Morales, J.F. / Cuello, L.G. / Zhao, Y. / Jogini, V. / Cortes, D.M. / Roux, B. / Perozo, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2atk.cif.gz | 113.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2atk.ent.gz | 91.4 KB | Display | PDB format |
PDBx/mmJSON format | 2atk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/at/2atk ftp://data.pdbj.org/pub/pdb/validation_reports/at/2atk | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules C
#3: Protein | Mass: 13153.546 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces lividans (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P0A334 |
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-Antibody , 2 types, 2 molecules AB
#1: Antibody | Mass: 23411.242 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) |
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#2: Antibody | Mass: 23435.738 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) |
-Non-polymers , 3 types, 51 molecules
#4: Chemical | ChemComp-K / #5: Chemical | ChemComp-F09 / | #6: Water | ChemComp-HOH / | |
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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: 3.8 Å3/Da / Density % sol: 67.59 % |
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Crystal grow | Temperature: 300 K / Method: vapor diffusion, sitting drop / pH: 5.4 Details: PEG400, KCl, MgAcetate, NaAcetate, pH 5.40, VAPOR DIFFUSION, SITTING DROP, temperature 300K |
-Data collection
Diffraction | Mean temperature: 150 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.1 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 19, 2005 |
Radiation | Monochromator: X29 beamline pptics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→50 Å / Num. all: 31306 / Num. obs: 27948 / % possible obs: 89.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 2.48→2.59 Å / % possible all: 91.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→50 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.5→50 Å
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