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Yorodumi- PDB-1abf: SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1abf | ||||||
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Title | SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES | ||||||
Components | L-ARABINOSE-BINDING PROTEIN | ||||||
Keywords | BINDING PROTEIN | ||||||
Function / homology | Function and homology information L-arabinose transmembrane transport / ABC-type monosaccharide transporter activity / monosaccharide binding / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / outer membrane-bounded periplasmic space / carbohydrate binding / membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Wilson, D.K. / Quiocho, F.A. | ||||||
Citation | Journal: Nature / Year: 1989 Title: Substrate specificity and affinity of a protein modulated by bound water molecules. Authors: Quiocho, F.A. / Wilson, D.K. / Vyas, N.K. #1: Journal: Nature / Year: 1984 Title: Novel Stereospecificity of the L-Arabinose-Binding Protein Authors: Quiocho, F.A. / Vyas, N.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1abf.cif.gz | 75.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1abf.ent.gz | 55.5 KB | Display | PDB format |
PDBx/mmJSON format | 1abf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1abf_validation.pdf.gz | 406.7 KB | Display | wwPDB validaton report |
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Full document | 1abf_full_validation.pdf.gz | 430.8 KB | Display | |
Data in XML | 1abf_validation.xml.gz | 11.2 KB | Display | |
Data in CIF | 1abf_validation.cif.gz | 16.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/1abf ftp://data.pdbj.org/pub/pdb/validation_reports/ab/1abf | HTTPS FTP |
-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: 33250.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P02924 |
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#2: Sugar | ChemComp-FCA / |
#3: Sugar | ChemComp-FCB / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.91 % | |||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: microdialysis / Details: referred to J.Mol.Biol. 86.491-493 1974 | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→10 Å /
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Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 10 Å / Num. reflection obs: 18780 / Rfactor obs: 0.134 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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