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- PDB-1opd: HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED B... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1opd | ||||||
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Title | HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D) | ||||||
![]() | HISTIDINE-CONTAINING PROTEIN | ||||||
![]() | PHOSPHOTRANSFERASE / HISTIDINE | ||||||
Function / homology | ![]() phosphotransferase activity, nitrogenous group as acceptor / regulation of carbon utilization / antisigma factor binding / positive regulation of glycogen catabolic process / phosphoenolpyruvate-dependent sugar phosphotransferase system / enzyme inhibitor activity / enzyme regulator activity / enzyme activator activity / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Napper, S. / Delbaere, L. / Waygood, B. | ||||||
![]() | ![]() Title: Mutation of serine-46 to aspartate in the histidine-containing protein of Escherichia coli mimics the inactivation by phosphorylation of serine-46 in HPrs from gram-positive bacteria. Authors: Napper, S. / Anderson, J.W. / Georges, F. / Quail, J.W. / Delbaere, L.T. / Waygood, E.B. #1: ![]() Title: Influence of N-CAP Mutations on the Structure and Stability of Escherichia Coli Hpr Authors: Thapar, R. / Nicholson, E.M. / Rajagopal, P. / Waygood, E.B. / Scholtz, J.M. / Klevit, R.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 28.3 KB | Display | ![]() |
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PDB format | ![]() | 18.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 420.2 KB | Display | ![]() |
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Full document | ![]() | 420.3 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 7.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 9158.327 Da / Num. of mol.: 1 / Mutation: S46D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.82 Å3/Da / Density % sol: 32.57 % | |||||||||||||||
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Crystal grow | *PLUS Temperature: 14 ℃ / pH: 4.6 / Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 21, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.927 Å / Relative weight: 1 |
Reflection | Num. obs: 10525 / % possible obs: 93.4 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rmerge(I) obs: 0.029 |
Reflection | *PLUS Highest resolution: 1.5 Å |
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Processing
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Refinement | Resolution: 1.5→8 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.5→8 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |