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Yorodumi- PDB-1fwp: CHEY-BINDING DOMAIN OF CHEA (RESIDUES 159-227), NMR, MINIMIZED AV... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1fwp | ||||||
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| Title | CHEY-BINDING DOMAIN OF CHEA (RESIDUES 159-227), NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
Components | CHEA | ||||||
Keywords | CHEMOTAXIS / KINASE / SIGNAL TRANSDUCTION | ||||||
| Function / homology | Function and homology informationnegative regulation of protein modification process / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / protein histidine kinase activity / thermotaxis / regulation of chemotaxis / phosphorelay sensor kinase activity ...negative regulation of protein modification process / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / protein histidine kinase activity / thermotaxis / regulation of chemotaxis / phosphorelay sensor kinase activity / histidine kinase / phosphorelay signal transduction system / establishment of localization in cell / chemotaxis / signal transduction / ATP binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Mcevoy, M.M. / Dahlquist, F.W. | ||||||
Citation | Journal: Biochemistry / Year: 1996Title: Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Authors: McEvoy, M.M. / Muhandiram, D.R. / Kay, L.E. / Dahlquist, F.W. #1: Journal: Biochemistry / Year: 1995Title: Nuclear Magnetic Resonance Assignments and Global Fold of a Chey-Binding Domain in Chea, the Chemotaxis-Specific Kinase of Escherichia Coli Authors: Mcevoy, M.M. / Zhou, H. / Roth, A.F. / Lowry, D.F. / Morrison, T.B. / Kay, L.E. / Dahlquist, F.W. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1fwp.cif.gz | 34.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1fwp.ent.gz | 23 KB | Display | PDB format |
| PDBx/mmJSON format | 1fwp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1fwp_validation.pdf.gz | 244 KB | Display | wwPDB validaton report |
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| Full document | 1fwp_full_validation.pdf.gz | 243.8 KB | Display | |
| Data in XML | 1fwp_validation.xml.gz | 4.9 KB | Display | |
| Data in CIF | 1fwp_validation.cif.gz | 5.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fw/1fwp ftp://data.pdbj.org/pub/pdb/validation_reports/fw/1fwp | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| NMR ensembles |
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Components
| #1: Protein | Mass: 15019.027 Da / Num. of mol.: 1 / Fragment: CHEY-BINDING DOMAIN, RESIDUES 159 - 227 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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Sample preparation
| Sample conditions | pH: 6.5 / Temperature: 303 K |
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| Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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| NMR software | Name: X-PLOR / Developer: BRUNGER / Classification: refinement | ||||||||
| NMR ensemble | Conformers submitted total number: 1 |
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