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Yorodumi- PDB-1mpb: MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mpb | ||||||
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Title | MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG) | ||||||
Components | MALTODEXTRIN-BINDING PROTEIN | ||||||
Keywords | PERIPLASMIC 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 | Shilton, B.H. / Mowbray, S.L. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: Crystal Structures and Solution Conformations of a Dominant-Negative Mutant of Escherichia Coli Maltose-Binding Protein Authors: Shilton, B.H. / Shuman, H.A. / Mowbray, S.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mpb.cif.gz | 108.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mpb.ent.gz | 85.2 KB | Display | PDB format |
PDBx/mmJSON format | 1mpb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mp/1mpb ftp://data.pdbj.org/pub/pdb/validation_reports/mp/1mpb | 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: 40724.137 Da / Num. of mol.: 1 / Mutation: W230R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Plasmid: PLH1 / Gene (production host): MALE671 / Production host: Escherichia coli (E. coli) / Strain (production host): HS3309 / References: UniProt: P02928, UniProt: P0AEX9*PLUS |
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#2: 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: 2.58 Å3/Da / Density % sol: 52.38 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6.2 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Sep 15, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→40 Å / Num. obs: 28060 / % possible obs: 96.5 % / Redundancy: 4.1 % / Rmerge(I) obs: 0.039 |
Reflection | *PLUS Highest resolution: 2 Å / % possible obs: 91.1 % / Observed criterion σ(I): 13 / Rmerge(I) obs: 0.039 |
-Processing
Software |
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Refinement | Resolution: 2→7.5 Å
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Displacement parameters | Biso mean: 25.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→7.5 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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