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Yorodumi- PDB-1jw5: Structure of Maltose Bound to Open-form Maltodextrin-binding Prot... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jw5 | |||||||||
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Title | Structure of Maltose Bound to Open-form Maltodextrin-binding Protein in P1 Crystal | |||||||||
Components | maltodextrin-binding protein | |||||||||
Keywords | SUGAR BINDING PROTEIN | |||||||||
Function / homology | Function and homology information detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / ATP-binding cassette (ABC) transporter complex / cell chemotaxis ...detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / 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 / Resolution: 2 Å | |||||||||
Authors | Duan, X. / Quiocho, F.A. | |||||||||
Citation | Journal: Biochemistry / Year: 2002 Title: Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands. Authors: Duan, X. / Quiocho, F.A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jw5.cif.gz | 90.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jw5.ent.gz | 66.9 KB | Display | PDB format |
PDBx/mmJSON format | 1jw5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jw/1jw5 ftp://data.pdbj.org/pub/pdb/validation_reports/jw/1jw5 | HTTPS FTP |
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-Related 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: 40753.152 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P02928, UniProt: P0AEX9*PLUS |
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#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose |
#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: 2.23 Å3/Da / Density % sol: 44.84 % | ||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.2 Details: PEG 20k, Mes, sodium azide, pH 6.2, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.6 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: May 14, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 42499 / % possible obs: 89 % / Observed criterion σ(I): 0 / Redundancy: 1.8 % / Rmerge(I) obs: 0.041 / Net I/σ(I): 18 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 1.2 % / Rmerge(I) obs: 0.041 / % possible all: 87.5 |
Reflection | *PLUS Lowest resolution: 30 Å / % possible obs: 89 % / Rmerge(I) obs: 0.042 |
-Processing
Software |
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Refinement | Resolution: 2→50 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2→50 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 50 Å / σ(F): 2 / Rfactor obs: 0.199 / Rfactor Rfree: 0.25 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||
Refine LS restraints | *PLUS
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