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Yorodumi- PDB-1km7: Solution Structure and Backbone Dynamics of GABARAP, GABAA Recept... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1km7 | ||||||
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Title | Solution Structure and Backbone Dynamics of GABARAP, GABAA Receptor Associated Protein | ||||||
Components | GABA(A) Receptor Associated Protein | ||||||
Keywords | PROTEIN BINDING / ubiquitin-like fold | ||||||
Function / homology | Function and homology information positive regulation of protein K48-linked ubiquitination / regulation of Rac protein signal transduction / GABA receptor binding / cellular response to nitrogen starvation / phosphatidylethanolamine binding / TBC/RABGAPs / microtubule associated complex / Macroautophagy / beta-tubulin binding / axoneme ...positive regulation of protein K48-linked ubiquitination / regulation of Rac protein signal transduction / GABA receptor binding / cellular response to nitrogen starvation / phosphatidylethanolamine binding / TBC/RABGAPs / microtubule associated complex / Macroautophagy / beta-tubulin binding / axoneme / smooth endoplasmic reticulum / autophagosome membrane / autophagosome assembly / extrinsic apoptotic signaling pathway via death domain receptors / autophagosome / protein targeting / sperm midpiece / macroautophagy / microtubule cytoskeleton organization / actin cytoskeleton / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / protein transport / chemical synaptic transmission / cytoplasmic vesicle / microtubule binding / microtubule / lysosome / Golgi membrane / synapse / ubiquitin protein ligase binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | Kouno, T. / Miura, K. / Tada, M. / Kanematsu, T. / Tate, S. / Shirakawa, M. / Hirata, M. / Kawano, K. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2002 Title: 1H, 13C and '5N resonance assignments of GABARAP, GABAA receptor associated protein. Authors: Kouno, T. / Miura, K. / Kanematsu, T. / Shirakawa, M. / Hirata, M. / Kawano, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1km7.cif.gz | 43.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1km7.ent.gz | 34.9 KB | Display | PDB format |
PDBx/mmJSON format | 1km7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/km/1km7 ftp://data.pdbj.org/pub/pdb/validation_reports/km/1km7 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13942.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX-2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: O95166 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 3D heteronuclear technicques. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 340 / pH: 6.5 / Pressure: 1 atm / Temperature: 298 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: distance geometry, simulated annealing / Software ordinal: 1 Details: This structure is based on a total of 976 restraints, 861 are NOE-derived distance constraints, 59 dihedral angle restraints, 56 distance restraints from hydrogen bonds. | ||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 1 |