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Yorodumi- PDB-1svx: Crystal structure of a designed selected Ankyrin Repeat protein i... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1svx | ||||||
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Title | Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein | ||||||
Components |
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Keywords | de novo protein/sugar binding protein / Ankyrin Repeat Protein / selected binder / Protein design / artificial complex / de novo protein-sugar binding protein COMPLEX | ||||||
Function / homology | Function and homology information detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis ...detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / outer membrane-bounded periplasmic space / periplasmic space / DNA damage response / membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.24 Å | ||||||
Authors | Binz, H.K. / Amstutz, P. / Kohl, A. / Stumpp, M.T. / Briand, C. / Forrer, P. / Gruetter, M.G. / Plueckthun, A. | ||||||
Citation | Journal: NAT.BIOTECHNOL. / Year: 2004 Title: High-affinity binders selected from designed ankyrin repeat protein libraries Authors: Binz, H.K. / Amstutz, P. / Kohl, A. / Stumpp, M.T. / Briand, C. / Forrer, P. / Gruetter, M.G. / Plueckthun, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1svx.cif.gz | 115.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1svx.ent.gz | 88.9 KB | Display | PDB format |
PDBx/mmJSON format | 1svx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sv/1svx ftp://data.pdbj.org/pub/pdb/validation_reports/sv/1svx | HTTPS FTP |
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-Related structure data
Related structure data | |
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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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-Components
#1: Protein | Mass: 18308.467 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Gene: designed synthetic gene / Plasmid: QE30 / Production host: Escherichia coli (E. coli) / Strain (production host): XL-1 blue / References: GenBank: 37576201 |
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#2: Protein | Mass: 43187.715 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: MALE, B4034, Z5632, ECS5017 / Plasmid: QE30 / Production host: Escherichia coli (E. coli) / Strain (production host): XL-1 blue / References: UniProt: P02928, UniProt: P0AEX9*PLUS |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 40.94 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 30% PEG 6000, 0.1M Tris, 0.1M NaCl, pH 8-9, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.24→25 Å / Num. obs: 22902 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.24→25 Å /
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Refinement step | Cycle: LAST / Resolution: 2.24→25 Å
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