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Yorodumi- PDB-1poh: THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTID... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1poh | ||||||
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Title | THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION | ||||||
Components | HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR | ||||||
Keywords | PHOSPHOTRANSFERASE | ||||||
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 regulator activity / enzyme activator activity / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Jia, Z. / Quail, W. / Delbaere, L. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1993 Title: The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination. Authors: Jia, Z. / Quail, J.W. / Waygood, E.B. / Delbaere, L.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1poh.cif.gz | 28.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1poh.ent.gz | 19.2 KB | Display | PDB format |
PDBx/mmJSON format | 1poh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1poh_validation.pdf.gz | 377.6 KB | Display | wwPDB validaton report |
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Full document | 1poh_full_validation.pdf.gz | 383.4 KB | Display | |
Data in XML | 1poh_validation.xml.gz | 4.3 KB | Display | |
Data in CIF | 1poh_validation.cif.gz | 6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/po/1poh ftp://data.pdbj.org/pub/pdb/validation_reports/po/1poh | HTTPS FTP |
-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: 9129.332 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0AA04 | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.73 Å3/Da / Density % sol: 28.97 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 14 ℃ / pH: 3.7 / Method: unknownDetails: referred to 'El-Kabbani', (1993) J.Biol.Chem., 262, 12926-12929 | ||||||||||||||||||||||||
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 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 10 Å / Num. obs: 4023 / % possible obs: 94.1 % / Num. measured all: 20532 / Rmerge(I) obs: 0.03 |
-Processing
Software |
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Refinement | Resolution: 2→8 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.135 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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