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Yorodumi- PDB-1pgy: Solution structure of the UBA domain in Saccharomyces cerevisiae ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1pgy | ||||||
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| Title | Solution structure of the UBA domain in Saccharomyces cerevisiae protein, Swa2p | ||||||
Components | Swa2p | ||||||
Keywords | PROTEIN BINDING / UBA / ubiquitin / Swa2 / auxilin / ubiquitin-associated domain | ||||||
| Function / homology | Function and homology informationendoplasmic reticulum inheritance / clathrin coat disassembly / clathrin-dependent endocytosis / clathrin binding / ubiquitin binding / vesicle / intracellular membrane-bounded organelle / endoplasmic reticulum membrane / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / molecular dynamics | ||||||
Authors | Chim, N. / Gall, W.E. / Xiao, J. / Harris, M.P. / Graham, T.R. / Krezel, A.M. | ||||||
Citation | Journal: PROTEINS: STRUCT.,FUNCT.,GENET. / Year: 2004Title: Solution structure of the ubiquitin-binding domain in Swa2p from Saccharomyces cerevisiae. Authors: Chim, N. / Gall, W.E. / Xiao, J. / Harris, M.P. / Graham, T.R. / Krezel, A.M. | ||||||
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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 | 1pgy.cif.gz | 303.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1pgy.ent.gz | 253 KB | Display | PDB format |
| PDBx/mmJSON format | 1pgy.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pg/1pgy ftp://data.pdbj.org/pub/pdb/validation_reports/pg/1pgy | HTTPS FTP |
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-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 5547.265 Da / Num. of mol.: 1 / Fragment: Ubiquitin-associated (UBA) domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SWA2 / Plasmid: pET32-EkLIC / Species (production host): Escherichia coli / Production host: ![]() |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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| NMR experiment |
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Sample preparation
| Details |
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| Sample conditions | Ionic strength: 50mM phosphate buffer / pH: 6 / Pressure: ambient / Temperature: 303 K | |||||||||||||||
| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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| Radiation wavelength | Relative weight: 1 | |||||||||||||||
| NMR spectrometer |
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Processing
| NMR software |
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| Refinement | Method: molecular dynamics / Software ordinal: 1 Details: 373 NOE-derived distance constraints, 34 residual dipolar couplings | ||||||||||||||||||||||||
| NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
| NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 |
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