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Yorodumi- PDB-1e2b: NMR STRUCTURE OF THE C10S MUTANT OF ENZYME IIB CELLOBIOSE OF THE ... -
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-Basic information
Entry | Database: PDB / ID: 1e2b | ||||||
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Title | NMR STRUCTURE OF THE C10S MUTANT OF ENZYME IIB CELLOBIOSE OF THE PHOSPHOENOL-PYRUVATE DEPENDENT PHOSPHOTRANSFERASE SYSTEM OF ESCHERICHIA COLI, 17 STRUCTURES | ||||||
Components | ENZYME IIB-CELLOBIOSE | ||||||
Keywords | TRANSFERASE / ENZYME IIB-CELLOBIOSE / PHOSPHOTRANSFERASE SYSTEM / SUGAR TRANSPORT / PHOSPHORYLATION | ||||||
Function / homology | Function and homology information protein-Npi-phosphohistidine-N,N'-diacetylchitobiose phosphotransferase / protein-phosphocysteine-N,N'-diacetylchitobiose phosphotransferase system transporter activity / N,N'-diacetylchitobiose import / protein-N(PI)-phosphohistidine-sugar phosphotransferase activity / phosphoenolpyruvate-dependent sugar phosphotransferase system / transmembrane transporter complex / kinase activity / phosphorylation / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, RESTRAINED MOLECULAR DYNAMICS, SIMULATED ANNEALING | ||||||
Authors | Ab, E. / Schuurman-Wolters, G. / Reizer, J. / Saier, M.H. / Dijkstra, K. / Scheek, R.M. / Robillard, G.T. | ||||||
Citation | Journal: Protein Sci. / Year: 1997 Title: The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Authors: Ab, E. / Schuurman-Wolters, G. / Reizer, J. / Saier, M.H. / Dijkstra, K. / Scheek, R.M. / Robillard, G.T. #1: Journal: Protein Sci. / Year: 1994 Title: Enzyme Iibcellobiose of the Phosphoenol-Pyruvate-Dependent Phosphotransferase System of Escherichia Coli: Backbone Assignment and Secondary Structure Determined by Three-Dimensional NMR Spectroscopy Authors: Ab, E. / Schuurman-Wolters, G.K. / Saier, M.H. / Reizer, J. / Jacuinod, M. / Roepstorff, P. / Dijkstra, K. / Scheek, R.M. / Robillard, G.T. #2: Journal: Genetics / Year: 1990 Title: Characterization and Nucleotide Sequence of the Cryptic Cel Operon of Escherichia Coli K12 Authors: Parker, L.L. / Hall, B.G. #3: Journal: Res.Microbiol. / Year: 1990 Title: The Cellobiose Permease of Escherichia Coli Consists of Three Proteins and is Homologous to the Lactose Permease of Staphylococcus Aureus Authors: Reizer, J. / Reizer, A. / Saier Junior, M.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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PDBx/mmCIF format | 1e2b.cif.gz | 545.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e2b.ent.gz | 469.7 KB | Display | PDB format |
PDBx/mmJSON format | 1e2b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e2/1e2b ftp://data.pdbj.org/pub/pdb/validation_reports/e2/1e2b | 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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NMR ensembles |
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-Components
#1: Protein | Mass: 11423.449 Da / Num. of mol.: 1 / Mutation: C10S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Cellular location: CYTOPLASM / Gene: CELA / Plasmid: PJR-IIBC10S / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM Production host: Escherichia coli str. K12 substr. W3110 (bacteria) Strain (production host): W3110 References: UniProt: P69795, protein-Npi-phosphohistidine-sugar phosphotransferase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: NOESY |
-Sample preparation
Sample conditions | pH: 6.18 / Temperature: 293 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, RESTRAINED MOLECULAR DYNAMICS, SIMULATED ANNEALING Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: TARGET FUNCTION, NUMBER OF VIOLATIONS Conformers calculated total number: 32 / Conformers submitted total number: 17 |