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- PDB-2hpr: HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR MUTANT WITH MET 5... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hpr | ||||||
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Title | HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR MUTANT WITH MET 51 REPLACED BY VAL AND SER 83 REPLACED BY CYS (M51V, S83C) | ||||||
![]() | HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR | ||||||
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Function / homology | ![]() regulation of carbohydrate utilization / phosphoenolpyruvate-dependent sugar phosphotransferase system / ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Herzberg, O. | ||||||
![]() | ![]() Title: Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins. Authors: Liao, D.I. / Herzberg, O. #1: ![]() Title: Structure of the Histidine-Containing Phosphocarrier Protein Hpr from Bacillus Subtilis at 2.0-Angstroms Resolution Authors: Herzberg, O. / Reddy, P. / Sutrina, S. / Saier Junior, M.H. / Reizer, J. / Kapadia, G. #2: ![]() Title: Crystallization of the Bacillus Subtilis Histidine-Containing Phosphocarrier Protein Hpr and Some of its Site-Directed Mutants Authors: Kapadia, G. / Reizer, J. / Sutrina, S. / Saier Junior, M.H. / Reddy, P. / Herzberg, O. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 29.6 KB | Display | ![]() |
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PDB format | ![]() | 19.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 9067.139 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / ![]() |
#3: Water | ChemComp-HOH / ![]() |
Compound details | SECONDARY STRUCTURE SPECIFICATIONS ARE BASED ON THE USE OF DSSP OF W. KABSCH AND C. SANDER ...SECONDARY STRUCTURE SPECIFICAT |
Sequence details | THE WILD-TYPE PROTEIN HAS 88 AMINO ACID RESIDUES. THE STRUCTURE PRESENTED IN THIS ENTRY IS OF AN ...THE WILD-TYPE PROTEIN HAS 88 AMINO ACID RESIDUES. THE STRUCTURE PRESENTED IN THIS ENTRY IS OF AN ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.16 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Method: vapor diffusion / PH range low: 6.4 / PH range high: 6.2 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 5083 / % possible obs: 90 % / Rmerge F obs: 0.086 |
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Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.1 Å / % possible obs: 58 % |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Rfactor obs: 0.145 / Highest resolution: 2 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 8 Å / Num. reflection obs: 4496 / σ(F): 2 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS Biso mean: 19.8 Å2 |