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Yorodumi- PDB-1opd: HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED B... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1opd | ||||||
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Title | HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D) | ||||||
Components | HISTIDINE-CONTAINING PROTEIN | ||||||
Keywords | PHOSPHOTRANSFERASE / HISTIDINE | ||||||
Function / homology | Function and homology information 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 activator activity / enzyme regulator activity / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.5 Å | ||||||
Authors | Napper, S. / Delbaere, L. / Waygood, B. | ||||||
Citation | Journal: Biochemistry / Year: 1996 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: Journal: Biochemistry / Year: 1996 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1opd.cif.gz | 28.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1opd.ent.gz | 18.4 KB | Display | PDB format |
PDBx/mmJSON format | 1opd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/op/1opd ftp://data.pdbj.org/pub/pdb/validation_reports/op/1opd | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Escherichia coli (E. coli) / Strain: ESK108 / Plasmid: PUC19 / Gene (production host): PTSH / Production host: Escherichia coli (E. coli) / Strain (production host): ESK108 / References: UniProt: P0AA04 |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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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: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.927 |
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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 |
-Processing
Software |
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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: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |