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Open data
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Basic information
Entry | Database: PDB / ID: 1cm2 | ||||||
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Title | STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES. | ||||||
![]() | HISTIDINE-CONTAINING PROTEIN | ||||||
![]() | TRANSFERASE / PHOSPHOTRANSFERASE / SUCCINIMIDE / ISOIMIDE | ||||||
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.T.J. / Waygood, E.B. | ||||||
![]() | ![]() Title: The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a ...Title: The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization Authors: Napper, S. / Delbaere, L.T. / Waygood, E.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 32.2 KB | Display | ![]() |
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PDB format | ![]() | 22 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 411.4 KB | Display | ![]() |
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Full document | ![]() | 412.1 KB | Display | |
Data in XML | ![]() | 6.1 KB | Display | |
Data in CIF | ![]() | 7.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 9106.273 Da / Num. of mol.: 1 / Mutation: HIS15ASP Source method: isolated from a genetically manipulated source Details: THE STRUCTURE IS THAT OF HIS15ASP HPR WHICH HAS UNDERGONE HYDROLYSIS FROM A HIGH-PI RINGED SPECIES OF THE PROTEIN WHICH IS BELIEVED TO INVOLVE SUCCINIMIDE OR ISOIMIDE FORMATION. Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.73 Å3/Da / Density % sol: 28.75 % | |||||||||||||||
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Crystal grow | pH: 4.6 / Details: pH 4.6 | |||||||||||||||
Crystal grow | *PLUS Temperature: 14 ℃ / pH: 4.4 / Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 273 K |
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Diffraction source | Source: ![]() ![]() ![]() ![]() ![]() |
Detector | Type: WEISSENBERG |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→10 Å / Num. obs: 6570 / % possible obs: 97.5 % / Observed criterion σ(I): 0 / Redundancy: 2.1 % / Rmerge(I) obs: 0.07 / Rsym value: 9.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: WILD TYPE E. COLI HPR Resolution: 1.8→10 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 10 Å / σ(F): 0 / Rfactor obs: 0.2 / Rfactor Rwork: 0.2 / Num. reflection obs: 5670 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.4 |