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Yorodumi- PDB-2hpr: HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR MUTANT WITH MET 5... -
+Open data
-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) | ||||||
Components | HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR | ||||||
Keywords | PHOSPHOTRANSFERASE | ||||||
Function / homology | Function and homology information regulation of carbohydrate utilization / phosphoenolpyruvate-dependent sugar phosphotransferase system / cytoplasm Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Herzberg, O. | ||||||
Citation | Journal: Structure / Year: 1994 Title: Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins. Authors: Liao, D.I. / Herzberg, O. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1992 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: Journal: J.Mol.Biol. / Year: 1990 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hpr.cif.gz | 29.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hpr.ent.gz | 19.5 KB | Display | PDB format |
PDBx/mmJSON format | 2hpr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2hpr_validation.pdf.gz | 385.2 KB | Display | wwPDB validaton report |
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Full document | 2hpr_full_validation.pdf.gz | 385.5 KB | Display | |
Data in XML | 2hpr_validation.xml.gz | 3.7 KB | Display | |
Data in CIF | 2hpr_validation.cif.gz | 5.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hp/2hpr ftp://data.pdbj.org/pub/pdb/validation_reports/hp/2hpr | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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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.) Bacillus subtilis (bacteria) / References: UniProt: P08877 |
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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: X-RAY DIFFRACTION |
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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 % |
-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 |