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Yorodumi- PDB-1qul: PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY THR COM... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qul | ||||||
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Title | PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY THR COMPLEX WITH CHLORINE AND PHOSPHATE | ||||||
Components | PHOSPHATE-BINDING PROTEIN | ||||||
Keywords | PHOSPHATE TRANSPORT / BINDING PROTEIN | ||||||
Function / homology | Function and homology information regulation of phosphatase activity / phosphate ion transport / phosphate ion transmembrane transport / phosphate ion binding / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / response to radiation / outer membrane-bounded periplasmic space / DNA damage response / membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.7 Å | ||||||
Authors | Yao, N. / Choudhary, A. / Ledvina, P.S. / Quiocho, F.A. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor. Authors: Yao, N. / Ledvina, P.S. / Choudhary, A. / Quiocho, F.A. #1: Journal: J.Biol.Chem. / Year: 1994 Title: Fine Tuning the Specificity of the Periplasmic Phosphate Transport Receptor. Site-Directed Mutagenesis, Ligand Binding, and Crystallographic Studies Authors: Wang, Z. / Choudhary, A. / Ledvina, P.S. / Quiocho, F.A. #2: Journal: Nature / Year: 1990 Title: High Specificity of a Phosphate Transport Protein Determined by Hydrogen Bonds Authors: Luecke, H. / 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 | 1qul.cif.gz | 76.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qul.ent.gz | 57 KB | Display | PDB format |
PDBx/mmJSON format | 1qul.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qul_validation.pdf.gz | 423.4 KB | Display | wwPDB validaton report |
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Full document | 1qul_full_validation.pdf.gz | 425 KB | Display | |
Data in XML | 1qul_validation.xml.gz | 15.7 KB | Display | |
Data in CIF | 1qul_validation.cif.gz | 23.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qu/1qul ftp://data.pdbj.org/pub/pdb/validation_reports/qu/1qul | 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: 34443.613 Da / Num. of mol.: 1 / Mutation: D137T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: PAN92 / References: UniProt: P06128, UniProt: P0AG82*PLUS |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-CL / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.07 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.5 / Method: vapor diffusion, hanging drop / Details: Wang, Z., (1994) J.Biol.Chem., 269, 25091. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SDMS / Detector: AREA DETECTOR / Date: Jan 9, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 37024 / % possible obs: 83 % / Observed criterion σ(I): 0 / Redundancy: 3 % / Rmerge(I) obs: 0.065 |
-Processing
Software |
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Refinement | Resolution: 1.7→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 8.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.72 |